› 2oc3

X-ray diffraction
1.5Å resolution

Crystal Structure of the Catalytic Domain of Human Protein Tyrosine Phosphatase non-receptor Type 18

Released:
DOI: 10.2210/pdb2oc3/pdb
PDB 2oc3 coloured by chain and viewed from the front.
PDB 2oc3 coloured by chain and viewed from the side.
PDB 2oc3 coloured by chain and viewed from the top.
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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 18 Chain: A
Molecule details ›
Chain: A
Length: 303 amino acids
Theoretical weight: 34.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99952 (Residues: 6-299; Coverage: 64%)
Gene names: BDP1, PTPN18
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: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 46.338Å b: 63.763Å c: 48.992Å
α: 90° β: 102.64° γ: 90°
R-values:
R R work R free
0.156 0.154 0.184
Expression system: Escherichia coli

Quick links

Citations

54 review citations

A Comprehensive Review of Receptor-Type Tyrosine-Protein Phosphatase Gamma (PTPRG) Role in Health and Non-Neoplastic Disease.
Boni et al. (2022)
53 more

7 mentions without citation

Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases.
Yu et al. (2007)
6 more