› 1zzw

X-ray diffraction
1.6Å resolution

Crystal Structure of catalytic domain of Human MAP Kinase Phosphatase 5

Released:
DOI: 10.2210/pdb1zzw/pdb
PDB entry 1zzw coloured by chain, front view.
PDB entry 1zzw coloured by chain, side view.
PDB entry 1zzw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase.
Jeong DG, Yoon TS, Kim JH, Shim MY, Jung SK, Son JH, Ryu SE, Kim SJ
J Mol Biol 360 946-55 (2006)
PMID: 16806267

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 149 amino acids
Theoretical weight: 17.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y6W6 (Residues: 320-467; Coverage: 31%)
Gene names: DUSP10, MKP5
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P1
Unit cell:
a: 39.533Å b: 41.073Å c: 55.569Å
α: 95.35° β: 99.81° γ: 117.35°
R-values:
R R work R free
0.196 0.193 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

The JNK signal transduction pathway.
Weston et al. (2007)
10 more

13 mentions without citation

DUSP8 phosphatase: structure, functions, expression regulation and the role in human diseases.
Ding et al. (2019)
12 more