› 5aes

X-ray diffraction
2.75Å resolution

Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase) in Complex with a PNP-derived Inhibitor

Released:
DOI: 10.2210/pdb5aes/pdb
PDB entry 5aes coloured by chain, front view.
PDB entry 5aes coloured by chain, side view.
PDB entry 5aes coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Synthesis of hydrolysis-resistant pyridoxal 5'-phosphate analogs and their biochemical and X-ray crystallographic characterization with the pyridoxal phosphatase chronophin.
Knobloch G, Jabari N, Stadlbauer S, Schindelin H, Köhn M, Gohla A
Bioorg Med Chem 23 2819-27 (2015)
PMID: 25783190

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158021 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chronophin Chains: A, B
Molecule details ›
Chains: A, B
Length: 293 amino acids
Theoretical weight: 31.61 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P60487 (Residues: 1-292; Coverage: 100%)
Gene names: Cin, Pdxp, Plp, Plpp
Sequence domains:
Structure domains: HAD superfamily/HAD-like

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand 5B0 2 x 5B0
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I23
Unit cell:
a: 166.81Å b: 166.81Å c: 166.81Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.247
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Pyridoxine-resveratrol hybrids Mannich base derivatives as novel dual inhibitors of AChE and MAO-B with antioxidant and metal-chelating properties for the treatment of Alzheimer's disease.
Yang et al. (2017)

4 mentions without citation

Pyrimidine Salvage Enzymes Are Essential for De Novo Biosynthesis of Deoxypyrimidine Nucleotides in Trypanosoma brucei.
Leija et al. (2016)
3 more