5hpe

X-ray diffraction
2.27Å resolution

Phosphatase domain of PP5 bound to a phosphomimetic Cdc37 substrate peptide

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-156701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hsp90 co-chaperone Cdc37, N-terminally processed; Serine/threonine-protein phosphatase 5 Chain: A
Molecule details ›
Chain: A
Length: 350 amino acids
Theoretical weight: 39.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53041 (Residues: 175-499; Coverage: 65%)
  • Canonical: Q16543 (Residues: 5-20; Coverage: 4%)
Gene names: CDC37, CDC37A, PPP5, PPP5C
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P212121
Unit cell:
a: 42.314Å b: 65.164Å c: 132.117Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.168 0.236
Expression system: Escherichia coli