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)
Assembly name:
Phosphoglycerate mutase 1 (preferred)
PDBe Complex ID:
PDB-CPX-148423 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate mutase 1
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 262 amino acids
Theoretical weight: 29.92 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: 262 amino acids
Theoretical weight: 29.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P18669 (Residues: 1-254; Coverage: 100%)
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like
