› 1q6n

X-ray diffraction
2.1Å resolution

THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEX WITH COMPOUND 4

Released:
DOI: 10.2210/pdb1q6n/pdb
PDB entry 1q6n coloured by chain, front view.
PDB entry 1q6n coloured by chain, side view.
PDB entry 1q6n coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structural basis for the selectivity of benzotriazole inhibitors of PTP1B.
Scapin G, Patel SB, Becker JW, Wang Q, Desponts C, Waddleton D, Skorey K, Cromlish W, Bayly C, Therien M, Gauthier JY, Li CS, Lau CK, Ramachandran C, Kennedy BP, Asante-Appiah E
Biochemistry 42 11451-9 (2003)
PMID: 14516196

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 310 amino acids
Theoretical weight: 36.24 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 MG 4 x MG
Ligand CL 2 x CL
Ligand P90 2 x P90
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 86.878Å b: 88.409Å c: 139.224Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Recent advances in protein tyrosine phosphatase 1B inhibitors.
Taylor et al. (2004)
6 more

4 mentions without citation

Reverse pharmacophore mapping and molecular docking studies for discovery of GTPase HRas as promising drug target for bis-pyrimidine derivatives.
Kumar et al. (2018)
3 more