› 4nwx

X-ray diffraction
2.01Å resolution

Crystal structure of phosphoglycerate mutase from Staphylococcus aureus in 2-phosphoglyceric acid bound form

Released:
DOI: 10.2210/pdb4nwx/pdb
PDB entry 4nwx coloured by chain, front view.
PDB entry 4nwx coloured by chain, side view.
PDB entry 4nwx coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus NCTC 8325
Primary publication:
Complete catalytic cycle of cofactor-independent phosphoglycerate mutase involves a spring-loaded mechanism.
Roychowdhury A, Kundu A, Bose M, Gujar A, Mukherjee S, Das AK
FEBS J 282 1097-110 (2015)
PMID: 25611430

Function and Biology Details

Reaction catalysed: 
2-phospho-D-glycerate = 3-phospho-D-glycerate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-557880 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase Chain: A
Molecule details ›
Chain: A
Length: 513 amino acids
Theoretical weight: 57.46 KDa
Source organism: Staphylococcus aureus subsp. aureus NCTC 8325
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2G029 (Residues: 1-505; Coverage: 100%)
Gene names: SAOUHSC_00798, gpmI
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 2PG 1 x 2PG
Ligand MN 2 x MN
Ligand DTT 1 x DTT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 73.639Å b: 83.206Å c: 89.073Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.216
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Structural and Functional Characterization of the BcsG Subunit of the Cellulose Synthase in Salmonella typhimurium.
Sun et al. (2018)
2 more

1 mention without citation

Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases.
Yu et al. (2017)