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:
Assembly name:
Bisphosphoglycerate mutase (preferred)
PDBe Complex ID:
PDB-CPX-139734 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bisphosphoglycerate mutase
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:
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like
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%)
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
X-ray source:
ESRF BEAMLINE ID14-4
Spacegroup:
P21
Expression system: Escherichia coli BL21(DE3)
