5muf

X-ray diffraction
3.1Å resolution

Crystal structure of human phosphoglycerate mutase family member 5 (PGAM5) in its enzymatically active dodecameric form induced by the presence of the N-terminal WDPNWD motif

Released:

Function and Biology Details

Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-188536 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase PGAM5, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 238 amino acids
Theoretical weight: 27.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96HS1 (Residues: 54-289; Coverage: 82%)
Gene name: PGAM5
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: I222
Unit cell:
a: 82.215Å b: 141.403Å c: 183.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.226 0.256
Expression system: Escherichia coli BL21(DE3)