X-ray diffraction
2.5Å resolution

Crystal structure of Human erythrocyte 2,3-bisphosphoglycerate mutase

Source organism: Homo sapiens
Primary publication:
Crystal structure of human bisphosphoglycerate mutase.
J. Biol. Chem. 279 39132-8 (2004)
PMID: 15258155

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Bisphosphoglycerate mutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 267 amino acids
Theoretical weight: 31.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P07738 (Residues: 1-259; Coverage: 100%)
Gene name: BPGM
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P21
Unit cell:
a: 38.638Å b: 61.768Å c: 123.333Å
α: 90° β: 94.99° γ: 90°
R R work R free
0.21 0.2 0.266
Expression system: Escherichia coli BL21(DE3)