PDBe 2h52

X-ray diffraction
2Å resolution

Crystal structure of human bisphosphoglycerate mutase complex with 3-phosphoglycerate (18 days)

Released:
Source organism: Homo sapiens
Entry authors: Wang Y, Gong W

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
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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 48.81Å b: 71.25Å c: 160.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.209
Expression system: Escherichia coli BL21(DE3)