2oyc

X-ray diffraction
1.72Å resolution

Crystal structure of human pyridoxal phosphate phosphatase

Released:

Function and Biology Details

Reactions catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Pyridoxal 5'-phosphate + H(2)O = pyridoxal + phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188517 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chronophin Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 33.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96GD0 (Residues: 2-296; Coverage: 100%)
Gene names: CIN, PDXP, PLP, PLPP
Sequence domains:
Structure domains: HAD superfamily/HAD-like

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P43212
Unit cell:
a: 54.329Å b: 54.329Å c: 213.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.192 0.223
Expression system: Escherichia coli BL21(DE3)