› 1c85

X-ray diffraction
2.72Å resolution

CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 2-(OXALYL-AMINO)-BENZOIC ACID

Released:
DOI: 10.2210/pdb1c85/pdb
PDB entry 1c85 coloured by chain, front view.
PDB entry 1c85 coloured by chain, side view.
PDB entry 1c85 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
2-(oxalylamino)-benzoic acid is a general, competitive inhibitor of protein-tyrosine phosphatases.
Andersen HS, Iversen LF, Jeppesen CB, Branner S, Norris K, Rasmussen HB, Møller KB, Møller NP
J Biol Chem 275 7101-8 (2000)
PMID: 10702277

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 1 Chain: A
Molecule details ›
Chain: A
Length: 298 amino acids
Theoretical weight: 34.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18031 (Residues: 1-298; Coverage: 69%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P3121
Unit cell:
a: 87.87Å b: 87.87Å c: 103.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.183 0.267
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Protein tyrosine phosphatase 1B inhibitors for diabetes.
Johnson et al. (2002)
11 more

5 mentions without citation

DeepAffinity: interpretable deep learning of compound-protein affinity through unified recurrent and convolutional neural networks.
Karimi et al. (2019)
4 more