4QYW

Structure of phosphono-CheY from T.maritima

PDB DOI: https://doi.org/10.2210/pdb4QYW/pdb

Classification: SIGNALING PROTEIN
Organism(s): Thermotoga maritima MSB8
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2014-07-25 Released: 2015-08-19
Deposition Author(s): Beyersdorf, M.S., Sircar, R., Crane, B.R., Halkides, C.J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.60 Å
R-Value Free: 0.268
R-Value Work: 0.218
R-Value Observed: 0.223

wwPDB Validation 3D Report Full Report

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

Literature

Isolation, Phosphonomethylation, and Crystallization of phosphono-CheY from Thermotoga maritima

Beyersdorf, M.S., Roebuck, J.A., Sircar, R., Pavlovsky, A., Crane, B.R., Halkides, C.J.

To be published.

Macromolecule Content

Total Structure Weight: 13.15 kDa
Atom Count: 995
Modelled Residue Count: 118
Deposited Residue Count: 119
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 CheY	A	119	Thermotoga maritima MSB8	Mutation(s): 2 Gene Names: cheY, TM_0700
UniProt
Find proteins for Q56312 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)) Explore Q56312 Go to UniProtKB: Q56312
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q56312
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
CYQ Query on CYQ	A	L-PEPTIDE LINKING	C₄ H₁₀ N O₅ P S		CYS

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.60 Å
R-Value Free: 0.268
R-Value Work: 0.218
R-Value Observed: 0.223
Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 49.729	α = 90
b = 61.126	β = 90
c = 33.285	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
CNS	refinement
HKL-2000	data collection
HKL-2000	data reduction
HKL-2000	data scaling
CNS	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2015-08-19

Deposition Author(s):

Beyersdorf, M.S.

Revision History (Full details and data files)

Version 1.0: 2015-08-19
Type: Initial release
Version 1.1: 2019-07-17
Changes: Data collection, Derived calculations, Refinement description

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.