4V9C

Allosteric control of the ribosome by small-molecule antibiotics

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.206 

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This is version 1.1 of the entry. See complete history. 


Literature

Allosteric control of the ribosome by small-molecule antibiotics.

Wang, L., Pulk, A., Wasserman, M.R., Feldman, M.B., Altman, R.B., Doudna Cate, J.H., Blanchard, S.C.

(2012) Nat Struct Mol Biol 19: 957-963

  • DOI: https://doi.org/10.1038/nsmb.2360
  • Primary Citation of Related Structures:  
    4V9C

  • PubMed Abstract: 

    Protein synthesis is targeted by numerous, chemically distinct antibiotics that bind and inhibit key functional centers of the ribosome. Using single-molecule imaging and X-ray crystallography, we show that the aminoglycoside neomycin blocks aminoacyl-transfer RNA (aa-tRNA) selection and translocation as well as ribosome recycling by binding to helix 69 (H69) of 23S ribosomal RNA within the large subunit of the Escherichia coli ribosome. There, neomycin prevents the remodeling of intersubunit bridges that normally accompanies the process of subunit rotation to stabilize a partially rotated ribosome configuration in which peptidyl (P)-site tRNA is constrained in a previously unidentified hybrid position. Direct measurements show that this neomycin-stabilized intermediate is incompatible with the translation factor binding that is required for distinct protein synthesis reactions. These findings reveal the functional importance of reversible intersubunit rotation to the translation mechanism and shed new light on the allosteric control of ribosome functions by small-molecule antibiotics.

    • Organizational Affiliation: 

    Department of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA.


Macromolecules

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S2B [auth AB],
DB [auth CB]		241Escherichia coli K-12Mutation(s): 0 
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Find proteins for P0A7V0 (Escherichia coli (strain K12))
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S3C [auth AC],
EB [auth CC]		233Escherichia coli K-12Mutation(s): 0 
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S4D [auth AD],
FB [auth CD]		206Escherichia coli K-12Mutation(s): 0 
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S5E [auth AE],
GB [auth CE]		167Escherichia coli K-12Mutation(s): 0 
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S6F [auth AF],
HB [auth CF]		135Escherichia coli K-12Mutation(s): 0 
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S7G [auth AG],
IB [auth CG]		179Escherichia coli K-12Mutation(s): 0 
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S8H [auth AH],
JB [auth CH]		130Escherichia coli K-12Mutation(s): 0 
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S9I [auth AI],
KB [auth CI]		130Escherichia coli K-12Mutation(s): 0 
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S10J [auth AJ],
LB [auth CJ]		103Escherichia coli K-12Mutation(s): 0 
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Entity ID: 11
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S11K [auth AK],
MB [auth CK]		129Escherichia coli K-12Mutation(s): 0 
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Entity ID: 12
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S12L [auth AL],
NB [auth CL]		124Escherichia coli K-12Mutation(s): 0 
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Entity ID: 13
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S13M [auth AM],
OB [auth CM]		118Escherichia coli K-12Mutation(s): 0 
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Entity ID: 14
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S14N [auth AN],
PB [auth CN]		101Escherichia coli K-12Mutation(s): 0 
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Entity ID: 15
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S15O [auth AO],
QB [auth CO]		89Escherichia coli K-12Mutation(s): 0 
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Entity ID: 16
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S16P [auth AP],
RB [auth CP]		82Escherichia coli K-12Mutation(s): 0 
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Entity ID: 17
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S17Q [auth AQ],
SB [auth CQ]		84Escherichia coli K-12Mutation(s): 0 
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Entity ID: 18
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S18R [auth AR],
TB [auth CR]		75Escherichia coli K-12Mutation(s): 0 
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Entity ID: 19
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S19S [auth AS],
UB [auth CS]		92Escherichia coli K-12Mutation(s): 0 
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Entity ID: 20
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S20T [auth AT],
VB [auth CT]		87Escherichia coli K-12Mutation(s): 0 
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Entity ID: 21
MoleculeChains Sequence LengthOrganismDetailsImage
30S ribosomal protein S21U [auth AU],
WB [auth CU]		71Escherichia coli K-12Mutation(s): 0 
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Entity ID: 26
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L2CC [auth DC],
Z [auth BC]		273Escherichia coli K-12Mutation(s): 0 
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Entity ID: 27
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L3AA [auth BD],
DC [auth DD]		209Escherichia coli K-12Mutation(s): 0 
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Entity ID: 28
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L4BA [auth BE],
EC [auth DE]		201Escherichia coli K-12Mutation(s): 0 
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Entity ID: 29
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L5CA [auth BF],
FC [auth DF]		179Escherichia coli K-12Mutation(s): 0 
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Entity ID: 30
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L6DA [auth BG],
GC [auth DG]		177Escherichia coli K-12Mutation(s): 0 
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Entity ID: 31
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L9EA [auth BH],
HC [auth DH]		149Escherichia coli K-12Mutation(s): 0 
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Entity ID: 32
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L11FA [auth BI],
IC [auth DI]		142Escherichia coli K-12Mutation(s): 0 
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Entity ID: 33
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L13GA [auth BJ],
JC [auth DJ]		142Escherichia coli K-12Mutation(s): 0 
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Entity ID: 34
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L14HA [auth BK],
KC [auth DK]		123Escherichia coli K-12Mutation(s): 0 
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Entity ID: 35
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L15IA [auth BL],
LC [auth DL]		144Escherichia coli K-12Mutation(s): 0 
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Entity ID: 36
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L16JA [auth BM],
MC [auth DM]		136Escherichia coli K-12Mutation(s): 0 
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Entity ID: 37
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L17KA [auth BN],
NC [auth DN]		127Escherichia coli K-12Mutation(s): 0 
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Entity ID: 38
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L18LA [auth BO],
OC [auth DO]		117Escherichia coli K-12Mutation(s): 0 
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Entity ID: 39
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L19MA [auth BP],
PC [auth DP]		115Escherichia coli K-12Mutation(s): 0 
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MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L20NA [auth BQ],
QC [auth DQ]		118Escherichia coli K-12Mutation(s): 0 
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Entity ID: 41
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L21OA [auth BR],
RC [auth DR]		103Escherichia coli K-12Mutation(s): 0 
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Entity ID: 42
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L22PA [auth BS],
SC [auth DS]		110Escherichia coli K-12Mutation(s): 0 
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Entity ID: 43
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L23QA [auth BT],
TC [auth DT]		100Escherichia coli K-12Mutation(s): 0 
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Entity ID: 44
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L24RA [auth BU],
UC [auth DU]		104Escherichia coli K-12Mutation(s): 0 
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Entity ID: 45
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L25SA [auth BV],
VC [auth DV]		94Escherichia coli K-12Mutation(s): 0 
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Entity ID: 46
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L27TA [auth BW],
WC [auth DW]		85Escherichia coli K-12Mutation(s): 0 
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Entity ID: 47
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L28UA [auth BX],
XC [auth DX]		78Escherichia coli K-12Mutation(s): 0 
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Entity ID: 48
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L29VA [auth BY],
YC [auth DY]		63Escherichia coli K-12Mutation(s): 0 
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UniProt GroupP0A7M6
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Entity ID: 49
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L30WA [auth BZ],
ZC [auth DZ]		59Escherichia coli K-12Mutation(s): 0 
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Entity ID: 50
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L32AD [auth D0],
XA [auth B0]		57Escherichia coli K-12Mutation(s): 0 
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Entity ID: 51
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L33BD [auth D1],
YA [auth B1]		55Escherichia coli K-12Mutation(s): 0 
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Entity ID: 52
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L34CD [auth D2],
ZA [auth B2]		46Escherichia coli K-12Mutation(s): 0 
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Entity ID: 53
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L35AB [auth B3],
DD [auth D3]		65Escherichia coli K-12Mutation(s): 0 
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Find proteins for P0A7Q1 (Escherichia coli (strain K12))
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UniProt GroupP0A7Q1
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Entity ID: 54
MoleculeChains Sequence LengthOrganismDetailsImage
50S ribosomal protein L36BB [auth B4],
ED [auth D4]		38Escherichia coli K-12Mutation(s): 0 
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Entity ID: 55
MoleculeChains Sequence LengthOrganismDetailsImage
Ribosome recycling factor, RRFZB [auth CY]185Escherichia coli K-12Mutation(s): 0 
UniProt
Find proteins for P0A805 (Escherichia coli (strain K12))
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Entity ID: 1
MoleculeChains LengthOrganismImage
16S ribosomal RNAA [auth AA],
CB [auth CA]		1,542Escherichia coli K-12
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Entity ID: 22
MoleculeChains LengthOrganismImage
Phenylalanine specific transfer RNA, tRNA-PheV [auth AV],
XB [auth CV]		76Escherichia coli K-12
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Entity ID: 23
MoleculeChains LengthOrganismImage
Messenger RNA, mRNAW [auth AX],
YB [auth CX]		24N/A
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Entity ID: 24
MoleculeChains LengthOrganismImage
23S ribosomal RNAAC [auth DA],
X [auth BA]		2,904Escherichia coli K-12
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Entity ID: 25
MoleculeChains LengthOrganismImage
5S ribosomal RNABC [auth DB],
Y [auth BB]		120Escherichia coli K-12
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Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NMY
Query on NMY
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CW [auth DA]
DW [auth DA]
EW [auth DA]
FW [auth DA]
GW [auth DA]
CW [auth DA],
DW [auth DA],
EW [auth DA],
FW [auth DA],
GW [auth DA],
HF [auth AA],
HW [auth DA],
IF [auth AA],
IW [auth DA],
JF [auth AA],
QL [auth BA],
RL [auth BA],
SL [auth BA],
TL [auth BA],
UL [auth BA],
VL [auth BA],
WL [auth BA],
ZO [auth CA]
NEOMYCIN
C23 H46 N6 O13
PGBHMTALBVVCIT-VCIWKGPPSA-N
ZN
Query on ZN
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FM [auth B4],
UW [auth D4]		ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
MG
Query on MG
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AE [auth AA]
AF [auth AA]
AG [auth BA]
AH [auth BA]
AI [auth BA]
AE [auth AA],
AF [auth AA],
AG [auth BA],
AH [auth BA],
AI [auth BA],
AJ [auth BA],
AK [auth BA],
AL [auth BA],
AM [auth BB],
AN [auth CA],
AO [auth CA],
AP [auth CX],
AQ [auth DA],
AR [auth DA],
AS [auth DA],
AT [auth DA],
AU [auth DA],
AV [auth DA],
AW [auth DA],
BE [auth AA],
BF [auth AA],
BG [auth BA],
BH [auth BA],
BI [auth BA],
BJ [auth BA],
BK [auth BA],
BL [auth BA],
BM [auth BB],
BN [auth CA],
BO [auth CA],
BP [auth DA],
BQ [auth DA],
BR [auth DA],
BS [auth DA],
BT [auth DA],
BU [auth DA],
BV [auth DA],
BW [auth DA],
CE [auth AA],
CF [auth AA],
CG [auth BA],
CH [auth BA],
CI [auth BA],
CJ [auth BA],
CK [auth BA],
CL [auth BA],
CM [auth BB],
CN [auth CA],
CO [auth CA],
CP [auth DA],
CQ [auth DA],
CR [auth DA],
CS [auth DA],
CT [auth DA],
CU [auth DA],
CV [auth DA],
DE [auth AA],
DF [auth AA],
DG [auth BA],
DH [auth BA],
DI [auth BA],
DJ [auth BA],
DK [auth BA],
DL [auth BA],
DM [auth BC],
DN [auth CA],
DO [auth CA],
DP [auth DA],
DQ [auth DA],
DR [auth DA],
DS [auth DA],
DT [auth DA],
DU [auth DA],
DV [auth DA],
EE [auth AA],
EF [auth AA],
EG [auth BA],
EH [auth BA],
EI [auth BA],
EJ [auth BA],
EK [auth BA],
EL [auth BA],
EM [auth BQ],
EN [auth CA],
EO [auth CA],
EP [auth DA],
EQ [auth DA],
ER [auth DA],
ES [auth DA],
ET [auth DA],
EU [auth DA],
EV [auth DA],
FD [auth AA],
FE [auth AA],
FF [auth AA],
FG [auth BA],
FH [auth BA],
FI [auth BA],
FJ [auth BA],
FK [auth BA],
FL [auth BA],
FN [auth CA],
FO [auth CA],
FP [auth DA],
FQ [auth DA],
FR [auth DA],
FS [auth DA],
FT [auth DA],
FU [auth DA],
FV [auth DA],
GD [auth AA],
GE [auth AA],
GF [auth AA],
GG [auth BA],
GH [auth BA],
GI [auth BA],
GJ [auth BA],
GK [auth BA],
GL [auth BA],
GM [auth CA],
GN [auth CA],
GO [auth CA],
GP [auth DA],
GQ [auth DA],
GR [auth DA],
GS [auth DA],
GT [auth DA],
GU [auth DA],
GV [auth DA],
HD [auth AA],
HE [auth AA],
HG [auth BA],
HH [auth BA],
HI [auth BA],
HJ [auth BA],
HK [auth BA],
HL [auth BA],
HM [auth CA],
HN [auth CA],
HO [auth CA],
HP [auth DA],
HQ [auth DA],
HR [auth DA],
HS [auth DA],
HT [auth DA],
HU [auth DA],
HV [auth DA],
ID [auth AA],
IE [auth AA],
IG [auth BA],
IH [auth BA],
II [auth BA],
IJ [auth BA],
IK [auth BA],
IL [auth BA],
IM [auth CA],
IN [auth CA],
IO [auth CA],
IP [auth DA],
IQ [auth DA],
IR [auth DA],
IS [auth DA],
IT [auth DA],
IU [auth DA],
IV [auth DA],
JD [auth AA],
JE [auth AA],
JG [auth BA],
JH [auth BA],
JI [auth BA],
JJ [auth BA],
JK [auth BA],
JL [auth BA],
JM [auth CA],
JN [auth CA],
JO [auth CA],
JP [auth DA],
JQ [auth DA],
JR [auth DA],
JS [auth DA],
JT [auth DA],
JU [auth DA],
JV [auth DA],
JW [auth DA],
KD [auth AA],
KE [auth AA],
KF [auth AD],
KG [auth BA],
KH [auth BA],
KI [auth BA],
KJ [auth BA],
KK [auth BA],
KL [auth BA],
KM [auth CA],
KN [auth CA],
KO [auth CA],
KP [auth DA],
KQ [auth DA],
KR [auth DA],
KS [auth DA],
KT [auth DA],
KU [auth DA],
KV [auth DA],
KW [auth DA],
LD [auth AA],
LE [auth AA],
LF [auth AN],
LG [auth BA],
LH [auth BA],
LI [auth BA],
LJ [auth BA],
LK [auth BA],
LL [auth BA],
LM [auth CA],
LN [auth CA],
LO [auth CA],
LP [auth DA],
LQ [auth DA],
LR [auth DA],
LS [auth DA],
LT [auth DA],
LU [auth DA],
LV [auth DA],
LW [auth DA],
MD [auth AA],
ME [auth AA],
MF [auth BA],
MG [auth BA],
MH [auth BA],
MI [auth BA],
MJ [auth BA],
MK [auth BA],
ML [auth BA],
MM [auth CA],
MN [auth CA],
MO [auth CA],
MP [auth DA],
MQ [auth DA],
MR [auth DA],
MS [auth DA],
MT [auth DA],
MU [auth DA],
MV [auth DA],
MW [auth DA],
ND [auth AA],
NE [auth AA],
NF [auth BA],
NG [auth BA],
NH [auth BA],
NI [auth BA],
NJ [auth BA],
NK [auth BA],
NL [auth BA],
NM [auth CA],
NN [auth CA],
NO [auth CA],
NP [auth DA],
NQ [auth DA],
NR [auth DA],
NS [auth DA],
NT [auth DA],
NU [auth DA],
NV [auth DA],
NW [auth DB],
OD [auth AA],
OE [auth AA],
OF [auth BA],
OG [auth BA],
OH [auth BA],
OI [auth BA],
OJ [auth BA],
OK [auth BA],
OL [auth BA],
OM [auth CA],
ON [auth CA],
OO [auth CA],
OP [auth DA],
OQ [auth DA],
OR [auth DA],
OS [auth DA],
OT [auth DA],
OU [auth DA],
OV [auth DA],
OW [auth DB],
PD [auth AA],
PE [auth AA],
PF [auth BA],
PG [auth BA],
PH [auth BA],
PI [auth BA],
PJ [auth BA],
PK [auth BA],
PL [auth BA],
PM [auth CA],
PN [auth CA],
PO [auth CA],
PP [auth DA],
PQ [auth DA],
PR [auth DA],
PS [auth DA],
PT [auth DA],
PU [auth DA],
PV [auth DA],
PW [auth DB],
QD [auth AA],
QE [auth AA],
QF [auth BA],
QG [auth BA],
QH [auth BA],
QI [auth BA],
QJ [auth BA],
QK [auth BA],
QM [auth CA],
QN [auth CA],
QO [auth CA],
QP [auth DA],
QQ [auth DA],
QR [auth DA],
QS [auth DA],
QT [auth DA],
QU [auth DA],
QV [auth DA],
QW [auth DB],
RD [auth AA],
RE [auth AA],
RF [auth BA],
RG [auth BA],
RH [auth BA],
RI [auth BA],
RJ [auth BA],
RK [auth BA],
RM [auth CA],
RN [auth CA],
RO [auth CA],
RP [auth DA],
RQ [auth DA],
RR [auth DA],
RS [auth DA],
RT [auth DA],
RU [auth DA],
RV [auth DA],
RW [auth DE],
SD [auth AA],
SE [auth AA],
SF [auth BA],
SG [auth BA],
SH [auth BA],
SI [auth BA],
SJ [auth BA],
SK [auth BA],
SM [auth CA],
SN [auth CA],
SO [auth CA],
SP [auth DA],
SQ [auth DA],
SR [auth DA],
SS [auth DA],
ST [auth DA],
SU [auth DA],
SV [auth DA],
SW [auth DL],
TD [auth AA],
TE [auth AA],
TF [auth BA],
TG [auth BA],
TH [auth BA],
TI [auth BA],
TJ [auth BA],
TK [auth BA],
TM [auth CA],
TN [auth CA],
TO [auth CA],
TP [auth DA],
TQ [auth DA],
TR [auth DA],
TS [auth DA],
TT [auth DA],
TU [auth DA],
TV [auth DA],
TW [auth DO],
UD [auth AA],
UE [auth AA],
UF [auth BA],
UG [auth BA],
UH [auth BA],
UI [auth BA],
UJ [auth BA],
UK [auth BA],
UM [auth CA],
UN [auth CA],
UO [auth CA],
UP [auth DA],
UQ [auth DA],
UR [auth DA],
US [auth DA],
UT [auth DA],
UU [auth DA],
UV [auth DA],
VD [auth AA],
VE [auth AA],
VF [auth BA],
VG [auth BA],
VH [auth BA],
VI [auth BA],
VJ [auth BA],
VK [auth BA],
VM [auth CA],
VN [auth CA],
VO [auth CA],
VP [auth DA],
VQ [auth DA],
VR [auth DA],
VS [auth DA],
VT [auth DA],
VU [auth DA],
VV [auth DA],
WD [auth AA],
WE [auth AA],
WF [auth BA],
WG [auth BA],
WH [auth BA],
WI [auth BA],
WJ [auth BA],
WK [auth BA],
WM [auth CA],
WN [auth CA],
WO [auth CA],
WP [auth DA],
WQ [auth DA],
WR [auth DA],
WS [auth DA],
WT [auth DA],
WU [auth DA],
WV [auth DA],
XD [auth AA],
XE [auth AA],
XF [auth BA],
XG [auth BA],
XH [auth BA],
XI [auth BA],
XJ [auth BA],
XK [auth BA],
XL [auth BA],
XM [auth CA],
XN [auth CA],
XO [auth CA],
XP [auth DA],
XQ [auth DA],
XR [auth DA],
XS [auth DA],
XT [auth DA],
XU [auth DA],
XV [auth DA],
YD [auth AA],
YE [auth AA],
YF [auth BA],
YG [auth BA],
YH [auth BA],
YI [auth BA],
YJ [auth BA],
YK [auth BA],
YL [auth BA],
YM [auth CA],
YN [auth CA],
YO [auth CA],
YP [auth DA],
YQ [auth DA],
YR [auth DA],
YS [auth DA],
YT [auth DA],
YU [auth DA],
YV [auth DA],
ZD [auth AA],
ZE [auth AA],
ZF [auth BA],
ZG [auth BA],
ZH [auth BA],
ZI [auth BA],
ZJ [auth BA],
ZK [auth BA],
ZL [auth BA],
ZM [auth CA],
ZN [auth CA],
ZP [auth DA],
ZQ [auth DA],
ZR [auth DA],
ZS [auth DA],
ZT [auth DA],
ZU [auth DA],
ZV [auth DA]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.206 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 212.18α = 90
b = 433.9β = 90
c = 608.03γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
PHENIXmodel building
XDSdata reduction
PHENIXphasing

Structure Validation

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Ligand Structure Quality Assessment 


View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-07-09
    Type: Initial release
  • Version 1.1: 2014-12-10
    Changes: Other