3P2L

Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.29 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.188 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis

Kim, Y.Zhou, M.Gu, M.Anderson, W.F.Joachimiak, A.Center for Structural Genomics of Infectious Diseases (CSGID)

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ATP-dependent Clp protease proteolytic subunit
A, B, C, D, E
A, B, C, D, E, F, G
201Francisella tularensis subsp. tularensis SCHU S4Mutation(s): 0 
Gene Names: clpPFTT_0624
EC: 3.4.21.92
UniProt
Find proteins for Q5NH47 (Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4))
Explore Q5NH47 
Go to UniProtKB:  Q5NH47
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5NH47
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 5 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PEG
Query on PEG

Download Ideal Coordinates CCD File 
BA [auth B]
CB [auth F]
DA [auth C]
DB [auth F]
EA [auth C]
BA [auth B],
CB [auth F],
DA [auth C],
DB [auth F],
EA [auth C],
GA [auth C],
GB [auth F],
I [auth A],
JB [auth G],
K [auth A],
KB [auth G],
LA [auth D],
LB [auth G],
M [auth A],
MA [auth D],
MB [auth G],
OA [auth D],
PB [auth G],
QA [auth D],
TA [auth E],
UA [auth E],
V [auth B],
VA [auth E],
W [auth B],
WA [auth E],
X [auth B]
DI(HYDROXYETHYL)ETHER
C4 H10 O3
MTHSVFCYNBDYFN-UHFFFAOYSA-N
PO4
Query on PO4

Download Ideal Coordinates CCD File 
AA [auth B]
AB [auth E]
HB [auth F]
JA [auth C]
NB [auth G]
AA [auth B],
AB [auth E],
HB [auth F],
JA [auth C],
NB [auth G],
R [auth A],
RA [auth D],
RB [auth G],
T [auth B],
U [auth B]
PHOSPHATE ION
O4 P
NBIIXXVUZAFLBC-UHFFFAOYSA-K
GOL
Query on GOL

Download Ideal Coordinates CCD File 
EB [auth F]
FA [auth C]
IA [auth C]
J [auth A]
L [auth A]
EB [auth F],
FA [auth C],
IA [auth C],
J [auth A],
L [auth A],
NA [auth D],
O [auth A],
PA [auth D],
Q [auth A],
QB [auth G],
XA [auth E],
Y [auth B],
YA [auth E],
Z [auth B],
ZA [auth E]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
EDO
Query on EDO

Download Ideal Coordinates CCD File 
FB [auth F],
HA [auth C],
N [auth A],
OB [auth G],
P [auth A]
1,2-ETHANEDIOL
C2 H6 O2
LYCAIKOWRPUZTN-UHFFFAOYSA-N
MG
Query on MG

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BB [auth F]
CA [auth C]
H [auth A]
IB [auth G]
KA [auth D]
BB [auth F],
CA [auth C],
H [auth A],
IB [auth G],
KA [auth D],
S [auth B],
SA [auth E]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B, C, D, E
A, B, C, D, E, F, G
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 120.523α = 90
b = 128.823β = 90
c = 98.03γ = 90
Software Package:
Software NamePurpose
SBC-Collectdata collection
HKL-3000data collection
HKL-3000phasing
SHELXSphasing
MLPHAREphasing
RESOLVEmodel building
SOLVEphasing
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling
RESOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-10-20
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance