X-ray diffraction
1.85Å resolution

Human bisphosphoglycerate mutase complex with 3-phosphoglycerate with crystal growth 90 days

Source organism: Homo sapiens
Primary publication:
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.
J. Biol. Chem. 281 39642-8 (2006)
PMID: 17052986

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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P212121
Unit cell:
a: 48.498Å b: 71.362Å c: 160.162Å
α: 90° β: 90° γ: 90°
R R work R free
0.18 0.18 0.215
Expression system: Escherichia coli BL21(DE3)