› 2fjm

X-ray diffraction
2.1Å resolution

The structure of phosphotyrosine phosphatase 1B in complex with compound 2

Released:
DOI: 10.2210/pdb2fjm/pdb
PDB entry 2fjm coloured by chain, front view.
PDB entry 2fjm coloured by chain, side view.
PDB entry 2fjm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformation-assisted inhibition of protein-tyrosine phosphatase-1B elicits inhibitor selectivity over T-cell protein-tyrosine phosphatase.
Asante-Appiah E, Patel S, Desponts C, Taylor JM, Lau C, Dufresne C, Therien M, Friesen R, Becker JW, Leblanc Y, Kennedy BP, Scapin G
J Biol Chem 281 8010-5 (2006)
PMID: 16407290

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-148259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 310 amino acids
Theoretical weight: 36.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

3 bound ligands:
Ligand CL 2 x CL
Ligand 073 2 x 073
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 86.431Å b: 86.621Å c: 139.193Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.192 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

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

2 mentions without citation

Structure Revision and Protein Tyrosine Phosphatase Inhibitory Activity of Drazepinone.
Cao et al. (2021)
1 more