› 3o0t

X-ray diffraction
1.9Å resolution

Crystal structure of human phosphoglycerate mutase family member 5 (PGAM5) in complex with phosphate

Released:
DOI: 10.2210/pdb3o0t/pdb
PDB entry 3o0t coloured by chain, front view.
PDB entry 3o0t coloured by chain, side view.
PDB entry 3o0t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of PGAM5 Provide Insight into Active Site Plasticity and Multimeric Assembly.
Chaikuad A, Filippakopoulos P, Marcsisin SR, Picaud S, Schröder M, Sekine S, Ichijo H, Engen JR, Takeda K, Knapp S
Structure 25 1089-1099.e3 (2017)
PMID: 28648608

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188537 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase PGAM5, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 202 amino acids
Theoretical weight: 23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96HS1 (Residues: 90-289; Coverage: 69%)
Gene name: PGAM5
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

2 bound ligands:
Ligand PO4 4 x PO4
Ligand EDO 11 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 70.96Å b: 73.09Å c: 81.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.228
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Recent Updates on Protein N-Phosphoramidate Hydrolases.
Jung et al. (2019)
3 more

2 mentions without citation

Defined PEG smears as an alternative approach to enhance the search for crystallization conditions and crystal-quality improvement in reduced screens.
Chaikuad et al. (2015)
1 more