› 3qcl

X-ray diffraction
2.4Å resolution

Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with 2-[(3,4-dichlorobenzyl)sulfanyl]-4-(4-hydroxybut-1-yn-1-yl)benzoic acid

Released:
DOI: 10.2210/pdb3qcl/pdb
PDB entry 3qcl coloured by chain, front view.
PDB entry 3qcl coloured by chain, side view.
PDB entry 3qcl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Small molecule receptor protein tyrosine phosphatase γ (RPTPγ) ligands that inhibit phosphatase activity via perturbation of the tryptophan-proline-aspartate (WPD) loop.
Sheriff S, Beno BR, Zhai W, Kostich WA, McDonnell PA, Kish K, Goldfarb V, Gao M, Kiefer SE, Yanchunas J, Huang Y, Shi S, Zhu S, Dzierba C, Bronson J, Macor JE, Appiah KK, Westphal RS, O'Connell J, Gerritz SW
J Med Chem 54 6548-62 (2011)
PMID: 21882820

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: 310 amino acids
Theoretical weight: 35.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23470 (Residues: 825-1128; Coverage: 21%)
Gene names: PTPG, PTPRG
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand NXV 1 x NXV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P3221
Unit cell:
a: 75.5Å b: 75.5Å c: 151.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.217 0.258
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Small molecule tools for functional interrogation of protein tyrosine phosphatases.
He et al. (2013)
3 more