› 3s4e

X-ray diffraction
1.26Å resolution

Crystal Structrue of a Novel Mitogen-activated Protein Kinase Phosphatase, SKRP1

Released:
DOI: 10.2210/pdb3s4e/pdb
PDB entry 3s4e coloured by chain, front view.
PDB entry 3s4e coloured by chain, side view.
PDB entry 3s4e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a novel mitogen-activated protein kinase phosphatase, SKRP1.
Wei CH, Ryu SY, Jeon YH, Yoon MY, Jeong DG, Kim SJ, Ryu SE
Proteins 79 3242-6 (2011)
PMID: 21989941

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:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186697 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 19 Chain: A
Molecule details ›
Chain: A
Length: 144 amino acids
Theoretical weight: 15.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WTR2 (Residues: 65-206; Coverage: 65%)
Gene names: DUSP17, DUSP19, LMWDSP3, SKRP1
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand PO4 1 x PO4
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P212121
Unit cell:
a: 46.852Å b: 50.313Å c: 57.872Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.15 0.181
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

The family-wide structure and function of human dual-specificity protein phosphatases.
Jeong et al. (2014)
2 more

1 mention without citation

Structural and Biochemical Analysis of Tyrosine Phosphatase Related to Biofilm Formation A (TpbA) from the Opportunistic Pathogen Pseudomonas aeruginosa PAO1.
Xu et al. (2015)