› 2nlk

X-ray diffraction
2.4Å resolution

Crystal structure of D1 and D2 catalytic domains of human Protein Tyrosine Phosphatase Gamma (D1+D2 PTPRG)

Released:
DOI: 10.2210/pdb2nlk/pdb
PDB entry 2nlk coloured by chain, front view.
PDB entry 2nlk coloured by chain, side view.
PDB entry 2nlk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Large-scale structural analysis of the classical human protein tyrosine phosphatome.
Barr AJ, Ugochukwu E, Lee WH, King ON, Filippakopoulos P, Alfano I, Savitsky P, Burgess-Brown NA, Müller S, Knapp S
Cell 136 352-63 (2009)
PMID: 19167335

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-149980 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor-type tyrosine-protein phosphatase gamma Chain: A
Molecule details ›
Chain: A
Length: 627 amino acids
Theoretical weight: 71.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23470 (Residues: 827-1445; Coverage: 43%)
Gene names: PTPG, PTPRG
Sequence domains: Protein-tyrosine phosphatase
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: RIGAKU
Spacegroup: P21212
Unit cell:
a: 118.51Å b: 133.996Å c: 59.084Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.237 0.274
Expression system: Escherichia coli

Quick links

Citations

58 review citations

Inside the human cancer tyrosine phosphatome.
Julien et al. (2011)
57 more

6 mentions without citation

Receptor protein tyrosine phosphatases and cancer: new insights from structural biology.
Nikolaienko et al. (2012)
5 more