› 4bx2

X-ray diffraction
2.19Å resolution

Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase) in complex with Beryllium trifluoride

Released:
DOI: 10.2210/pdb4bx2/pdb
PDB entry 4bx2 coloured by chain, front view.
PDB entry 4bx2 coloured by chain, side view.
PDB entry 4bx2 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Chronophin dimerization is required for proper positioning of its substrate specificity loop.
Kestler C, Knobloch G, Tessmer I, Jeanclos E, Schindelin H, Gohla A
J Biol Chem 289 3094-103 (2014)
PMID: 24338687

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 BEF 2 x BEF
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: I23
Unit cell:
a: 166.83Å b: 166.83Å c: 166.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Cofilin and Actin Dynamics: Multiple Modes of Regulation and Their Impacts in Neuronal Development and Degeneration.
Bamburg et al. (2021)
6 other articles

2 mentions without citation

Functional Diversity of Haloacid Dehalogenase Superfamily Phosphatases from Saccharomyces cerevisiae: BIOCHEMICAL, STRUCTURAL, AND EVOLUTIONARY INSIGHTS.
Kuznetsova et al. (2015)
1 more