5zrm

X-ray diffraction
2.28Å resolution

Phosphoglycerate mutase 1 complexed with a small molecule inhibitor In-AC

Released:
Source organism: Homo sapiens
Entry authors: Jiang LL, Zhou L

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-148422 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phosphoglycerate mutase 1 Chain: B
Molecule details ›
Chain: B
Length: 234 amino acids
Theoretical weight: 26.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18669 (Residues: 2-235; Coverage: 92%)
Gene names: CDABP0006, PGAM1, PGAMA
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like
Phosphoglycerate mutase 1 Chain: C
Molecule details ›
Chain: C
Length: 234 amino acids
Theoretical weight: 26.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18669 (Residues: 2-235; Coverage: 92%)
Gene names: CDABP0006, PGAM1, PGAMA
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P212121
Unit cell:
a: 82.421Å b: 82.971Å c: 103.841Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.196 0.232
Expression system: Escherichia coli