› 2qdm

X-ray diffraction
2.05Å resolution

Crystal structure of the HePTP catalytic domain C270S/D236A/Q314A mutant

Released:
DOI: 10.2210/pdb2qdm/pdb
PDB entry 2qdm coloured by chain, front view.
PDB entry 2qdm coloured by chain, side view.
PDB entry 2qdm coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Critton DA, Tortajada A, Page R

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-152862 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 7 Chain: A
Molecule details ›
Chain: A
Length: 309 amino acids
Theoretical weight: 35.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35236 (Residues: 65-360; Coverage: 82%)
Gene name: PTPN7
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: C2
Unit cell:
a: 119.324Å b: 39.041Å c: 83.473Å
α: 90° β: 124.53° γ: 90°
R-values:
R R work R free
0.166 0.164 0.208
Expression system: Escherichia coli

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Citations

5 review citations

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

2 mentions without citation

Structural basis of substrate recognition by hematopoietic tyrosine phosphatase.
Critton et al. (2008)
1 more