PDBe 1yfk

X-ray diffraction
2.7Å resolution

Crystal structure of human B type phosphoglycerate mutase

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human B-type phosphoglycerate mutase bound with citrate.
Biochem. Biophys. Res. Commun. 331 1207-15 (2005)
PMID: 15883004

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: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 29.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P21
Unit cell:
a: 42.861Å b: 65.745Å c: 124.812Å
α: 90° β: 94.36° γ: 90°
R-values:
R R work R free
0.218 0.216 0.255
Expression system: Escherichia coli BL21(DE3)