3QWD

Crystal structure of ClpP from Staphylococcus aureus

PDB DOI: https://doi.org/10.2210/pdb3QWD/pdb

Classification: HYDROLASE
Organism(s): Staphylococcus aureus subsp. aureus NCTC 8325
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2011-02-28 Released: 2011-05-18
Deposition Author(s): Geiger, S.R., Boettcher, T., Sieber, S.A., Cramer, P.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.10 ?
R-Value Free: 0.226
R-Value Work: 0.208
R-Value Observed: 0.209

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

A Conformational Switch Underlies ClpP Protease Function.

Geiger, S.R., Bottcher, T., Sieber, S.A., Cramer, P.

(2011) Angew Chem Int Ed Engl 50: 5749-5752

PubMed: 21544912 Search on PubMed
DOI: https://doi.org/10.1002/anie.201100666
Primary Citation of Related Structures:
3QWD

Organizational Affiliation

Gene Center and Department of Biochemistry, Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universit?t München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.

Macromolecule Content

Total Structure Weight: 316.35 kDa
Atom Count: 20,404
Modelled Residue Count: 2,589
Deposited Residue Count: 2,842
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
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	203	Staphylococcus aureus subsp. aureus NCTC 8325	Mutation(s): 0 Gene Names: clpP, SAOUHSC_00790 EC: 3.4.21.92
UniProt
Find proteins for Q2G036 (Staphylococcus aureus (strain NCTC 8325 / PS 47)) Explore Q2G036 Go to UniProtKB: Q2G036
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q2G036
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
CL Query on CL Download Ideal Coordinates CCD File SDF format, chain O [auth A] SDF format, chain P [auth B] SDF format, chain Q [auth C] SDF format, chain R [auth D] SDF format, chain S [auth L] SDF format, chain T [auth L] SDF format, chain U [auth M] MOL2 format, chain O [auth A] MOL2 format, chain P [auth B] MOL2 format, chain Q [auth C] MOL2 format, chain R [auth D] MOL2 format, chain S [auth L] MOL2 format, chain T [auth L] MOL2 format, chain U [auth M] mmCIF format, chain O [auth A] mmCIF format, chain P [auth B] mmCIF format, chain Q [auth C] mmCIF format, chain R [auth D] mmCIF format, chain S [auth L] mmCIF format, chain T [auth L] mmCIF format, chain U [auth M]	O [auth A] P [auth B] Q [auth C] R [auth D] S [auth L] O [auth A], P [auth B], Q [auth C], R [auth D], S [auth L], T [auth L], U [auth M]	CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M		Interactions Focus chain O [auth A] Focus chain P [auth B] Focus chain Q [auth C] Focus chain R [auth D] Focus chain S [auth L] Focus chain T [auth L] Focus chain U [auth M] Interactions & Density Focus chain O [auth A] Focus chain P [auth B] Focus chain Q [auth C] Focus chain R [auth D] Focus chain S [auth L] Focus chain T [auth L] Focus chain U [auth M]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.10 ?
R-Value Free: 0.226
R-Value Work: 0.208
R-Value Observed: 0.209
Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( ? )	Angle ( ? )
a = 172.048	α = 90
b = 177.974	β = 90
c = 100.278	γ = 90

Software Package:

Software Name	Purpose
ADSC	data collection
AMoRE	phasing
BUSTER	refinement
XDS	data reduction
XDS	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2011-05-18

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2011-05-18
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2024-02-21
Changes: Data collection, Database references, Derived calculations

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Deposit Data

Help and Resources

3QWD

Crystal structure of ClpP from Staphylococcus aureus

A Conformational Switch Underlies ClpP Protease Function.

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)