› 2oud

X-ray diffraction
2.8Å resolution

Crystal structure of the catalytic domain of human MKP5

Released:
DOI: 10.2210/pdb2oud/pdb
PDB entry 2oud coloured by chain, front view.
PDB entry 2oud coloured by chain, side view.
PDB entry 2oud coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5.
Tao X, Tong L
Protein Sci 16 880-6 (2007)
PMID: 17400920

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 10 Chain: A
Molecule details ›
Chain: A
Length: 177 amino acids
Theoretical weight: 20.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y6W6 (Residues: 315-482; Coverage: 35%)
Gene names: DUSP10, MKP5
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P3221
Unit cell:
a: 92.514Å b: 92.514Å c: 78.114Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.213 0.248
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Molecular basis of MAP kinase regulation.
Peti et al. (2013)
6 more

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)