PDBe 3nfy

X-ray diffraction
1.94Å resolution

The Structure of Human Bisphosphoglycerate Mutase to 1.94A

Released:
Source organism: Homo sapiens
Primary publication:
Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 1415-20 (2010)
PMID: 21045285

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

Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • 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: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 38.472Å b: 61.345Å c: 122.696Å
α: 90° β: 95.87° γ: 90°
R-values:
R R work R free
0.182 0.178 0.277
Expression system: Escherichia coli BL21(DE3)