› 5um0

X-ray diffraction
1.85Å resolution

Crystal structure of 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase from Neisseria gonorrhoeae

Released:
DOI: 10.2210/pdb5um0/pdb
PDB entry 5um0 coloured by chain, front view.
PDB entry 5um0 coloured by chain, side view.
PDB entry 5um0 coloured by chain, top view.
Source organism: Neisseria gonorrhoeae NCCP11945
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed: 
(1a) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-N(tau)-phospho-L-histidine + 2/3-phospho-D-glycerate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110106 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 235 amino acids
Theoretical weight: 27 KDa
Source organism: Neisseria gonorrhoeae NCCP11945
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B4RIY7 (Residues: 1-227; Coverage: 100%)
Gene names: NGK_0248, gpmA
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

1 bound ligand:
Ligand TLA 4 x TLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 71.58Å b: 73.03Å c: 96.93Å
α: 90° β: 97.6° γ: 90°
R-values:
R R work R free
0.167 0.166 0.209
Expression system: Escherichia coli BL21(DE3)

Quick links