3HM4

CRYSTAL STRUCTURE OF A CHEMOTAXIS PROTEIN CHEX (DDE_0281) FROM DESULFOVIBRIO DESULFURICANS SUBSP. AT 1.30 A RESOLUTION

PDB DOI: https://doi.org/10.2210/pdb3HM4/pdb

Classification: HYDROLASE
Organism(s): Oleidesulfovibrio alaskensis G20
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2009-05-28 Released: 2009-06-23
Deposition Author(s): Joint Center for Structural Genomics (JCSG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.30 Å
R-Value Free: 0.165
R-Value Work: 0.138
R-Value Observed: 0.139

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

Crystal structure of Chemotaxis protein CheX (YP_386777.1) from DESULFOVIBRIO DESULFURICANS G20 at 1.30 A resolution

Joint Center for Structural Genomics (JCSG)

To be published.

Macromolecule Content

Total Structure Weight: 33.22 kDa
Atom Count: 2,633
Modelled Residue Count: 303
Deposited Residue Count: 312
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Chemotaxis protein CheX	A, B	156	Oleidesulfovibrio alaskensis G20	Mutation(s): 0 Gene Names: Dde_0281, YP_386777.1
UniProt
Find proteins for Q316R4 (Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)) Explore Q316R4 Go to UniProtKB: Q316R4
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q316R4
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
GOL Query on GOL Download Ideal Coordinates CCD File SDF format, chain D [auth A] MOL2 format, chain D [auth A]	D [auth A]	GLYCEROL C₃ H₈ O₃ PEDCQBHIVMGVHV-UHFFFAOYSA-N		Interactions Focus chain D [auth A] Interactions & Density Focus chain D [auth A]
UNL Query on UNL Download Ideal Coordinates CCD File	C [auth A]	Unknown ligand PEDCQBHIVMGVHV-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A, B	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.30 Å
R-Value Free: 0.165
R-Value Work: 0.138
R-Value Observed: 0.139
Space Group: P 2₁ 2₁ 2₁
Diffraction Data: https://doi.org/10.18430/M33HM4

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 42.362	α = 90
b = 73.999	β = 90
c = 83.338	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
PHENIX	refinement
SHELX	phasing
MolProbity	model building
XSCALE	data scaling
PDB_EXTRACT	data extraction
XDS	data reduction
SHELXD	phasing
autoSHARP	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2009-06-23

Deposition Author(s):

Joint Center for Structural Genomics (JCSG)

Revision History (Full details and data files)

Version 1.0: 2009-06-23
Type: Initial release
Version 1.1: 2011-07-13
Changes: Non-polymer description, Version format compliance
Version 1.2: 2017-11-01
Changes: Refinement description
Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description
Version 1.4: 2023-02-01
Changes: Database references, Derived calculations

Prepare Data

Validate Data

Deposit Data

Help and Resources

3HM4

CRYSTAL STRUCTURE OF A CHEMOTAXIS PROTEIN CHEX (DDE_0281) FROM DESULFOVIBRIO DESULFURICANS SUBSP. AT 1.30 A RESOLUTION

Crystal structure of Chemotaxis protein CheX (YP_386777.1) from DESULFOVIBRIO DESULFURICANS G20 at 1.30 A resolution

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)