› 4qun

X-ray diffraction
1.86Å resolution

Crystal structure of the PTPN3 (PTPH1) catalytic domain C842S mutant

Released:
DOI: 10.2210/pdb4qun/pdb
PDB entry 4qun coloured by chain, front view.
PDB entry 4qun coloured by chain, side view.
PDB entry 4qun coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation.
Chen KE, Lin SY, Wu MJ, Ho MR, Santhanam A, Chou CC, Meng TC, Wang AH
Sci Signal 7 ra98 (2014)
PMID: 25314968

Function and Biology Details

Reaction catalysed: 
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-150655 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 306 amino acids
Theoretical weight: 34.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P26045 (Residues: 628-909; Coverage: 31%)
Gene names: PTPH1, PTPN3
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: C2221
Unit cell:
a: 94.74Å b: 97Å c: 138.207Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.177 0.206
Expression system: Escherichia coli

Quick links

Citations

4 review citations

p38γ and p38δ Mitogen Activated Protein Kinases (MAPKs), New Stars in the MAPK Galaxy.
Escós et al. (2016)
3 more

1 mention without citation

PTP-MEG2 regulates quantal size and fusion pore opening through two distinct structural bases and substrates.
Xu et al. (2021)