4zvz

X-ray diffraction
2Å resolution

Co-crystal structures of PP5 in complex with 5-methyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase 5 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 333 amino acids
Theoretical weight: 37.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53041 (Residues: 169-499; Coverage: 66%)
Gene names: PPP5, PPP5C
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P1
Unit cell:
a: 40.858Å b: 80.52Å c: 91.165Å
α: 88.15° β: 87.33° γ: 86.71°
R-values:
R R work R free
0.206 0.204 0.235
Expression system: Escherichia coli