› 2pq5

X-ray diffraction
2.3Å resolution

Crystal structure of Dual specificity protein phosphatase 13 (DUSP13)

Released:
DOI: 10.2210/pdb2pq5/pdb
PDB entry 2pq5 coloured by chain, front view.
PDB entry 2pq5 coloured by chain, side view.
PDB entry 2pq5 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Ugochukwu E, Salah E, Savitsky P, Barr A, Pantic N, Niesen F, Burgess-Brown N, Berridge G, Bunkoczi G, Uppenberg J, Pike ACW, Sundstrom M, Arrowsmith CH, Weigelt J, Edwards A, von Delft F, Knapp S, Structural Genomics Consortium (SGC)

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193789 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 13B Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 205 amino acids
Theoretical weight: 23.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UII6 (Residues: 1-198; Coverage: 100%)
Gene names: DUSP13, DUSP13B, SKRP4, TMDP
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3121
Unit cell:
a: 73.821Å b: 73.821Å c: 303.803Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.176 0.26
Expression system: Escherichia coli

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