PDBe 4gpi

X-ray diffraction
2.08Å resolution

Crystal structure of human B type phosphoglycerate mutase

Released:

Function and Biology Details

Reactions catalysed:
(1a) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-N(tau)-phospho-L-histidine + 2/3-phospho-D-glycerate
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate mutase 1 Chains: B, C
Molecule details ›
Chains: B, C
Length: 262 amino acids
Theoretical weight: 29.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18669 (Residues: 1-254; Coverage: 100%)
Gene names: CDABP0006, PGAM1, PGAMA
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 81.662Å b: 80.263Å c: 89.275Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.232
Expression system: Escherichia coli