3Q7H

Structure of the ClpP subunit of the ATP-dependent Clp Protease from Coxiella burnetii


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.170 
  • R-Value Observed: 0.172 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structure of the ClpP subunit of the ATP-dependent Clp Protease from Coxiella burnetii

Anderson, S.M.Wawrzak, Z.Gordon, E.Hasseman, J.Anderson, W.F.Savchenko, 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, H, I, J, K, L, M, N
195Coxiella burnetii RSA 331Mutation(s): 0 
Gene Names: clpPCOXBURSA331_A1213
EC: 3.4.21.92
UniProt
Find proteins for Q83DJ2 (Coxiella burnetii (strain RSA 493 / Nine Mile phase I))
Explore Q83DJ2 
Go to UniProtKB:  Q83DJ2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ83DJ2
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PEG
Query on PEG

Download Ideal Coordinates CCD File 
CA [auth D]
CB [auth J]
DB [auth J]
EB [auth J]
FA [auth E]
CA [auth D],
CB [auth J],
DB [auth J],
EB [auth J],
FA [auth E],
HB [auth K],
IB [auth K],
JA [auth F],
LB [auth L],
MA [auth G],
MB [auth L],
NA [auth G],
O [auth A],
P [auth A],
PB [auth M],
Q [auth A],
QA [auth H],
QB [auth M],
RA [auth H],
S [auth B],
SA [auth H],
T [auth B],
TA [auth H],
TB [auth N],
U [auth B],
UB [auth N],
WA [auth I],
X [auth C],
XA [auth I],
Y [auth C],
YA [auth I],
Z [auth C],
ZA [auth I]
DI(HYDROXYETHYL)ETHER
C4 H10 O3
MTHSVFCYNBDYFN-UHFFFAOYSA-N
CA
Query on CA

Download Ideal Coordinates CCD File 
AA [auth C]
AB [auth I]
BA [auth C]
BB [auth I]
DA [auth D]
AA [auth C],
AB [auth I],
BA [auth C],
BB [auth I],
DA [auth D],
EA [auth D],
FB [auth J],
GA [auth E],
GB [auth J],
HA [auth E],
IA [auth E],
JB [auth K],
KA [auth F],
KB [auth K],
LA [auth F],
NB [auth L],
OA [auth G],
OB [auth L],
PA [auth G],
R [auth A],
RB [auth M],
SB [auth M],
UA [auth H],
V [auth B],
VA [auth H],
VB [auth N],
W [auth B],
WB [auth N]
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-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, H, I, J, K, L, M, N
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 101.912α = 90
b = 137.469β = 109.03
c = 127.784γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
PDB_EXTRACTdata extraction
BLU-MAXdata collection
HKL-2000data reduction
HKL-2000data scaling
SHELXSphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2011-01-12
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance