1R5J

Crystal Structure of a Phosphotransacetylase from Streptococcus pyogenes

PDB DOI: https://doi.org/10.2210/pdb1R5J/pdb

Classification: TRANSFERASE
Organism(s): Streptococcus pyogenes
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2003-10-10 Released: 2004-04-13
Deposition Author(s): Xu, Q.S., Shin, D.H., Pufan, R., Yokota, H., Kim, R., Kim, S.H., Berkeley Structural Genomics Center (BSGC)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.70 Å
R-Value Free: 0.281
R-Value Work: 0.229
R-Value Observed: 0.229

wwPDB Validation 3D Report Full Report

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

Literature

Crystal structure of a phosphotransacetylase from Streptococcus pyogenes.

Xu, Q.S., Shin, D.H., Pufan, R., Yokota, H., Kim, R., Kim, S.H.

(2004) Proteins 55: 479-481

PubMed: 15048838 Search on PubMed
DOI: https://doi.org/10.1002/prot.20039
Primary Citation of Related Structures:
1R5J

Organizational Affiliation

Berkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.

Macromolecule Content

Total Structure Weight: 73.35 kDa
Atom Count: 5,034
Modelled Residue Count: 658
Deposited Residue Count: 674
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
putative phosphotransacetylase	A, B	337	Streptococcus pyogenes	Mutation(s): 10 EC: 2.3.1.8
UniProt
Find proteins for Q99ZQ5 (Streptococcus pyogenes serotype M1) Explore Q99ZQ5 Go to UniProtKB: Q99ZQ5
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q99ZQ5
Sequence Annotations Expand
Reference Sequence

Small Molecules

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: 2.70 Å
R-Value Free: 0.281
R-Value Work: 0.229
R-Value Observed: 0.229
Space Group: P 4₃ 3 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 173.725	α = 90
b = 173.725	β = 90
c = 173.725	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
HKL-2000	data reduction
SCALEPACK	data scaling
SOLVE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2004-04-13

Deposition Author(s):

Berkeley Structural Genomics Center (BSGC)

Revision History (Full details and data files)

Version 1.0: 2004-04-13
Type: Initial release
Version 1.1: 2008-04-29
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

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.