› 1lqf

X-ray diffraction
2.5Å resolution

Structure of PTP1b in Complex with a Peptidic Bisphosphonate Inhibitor

Released:
DOI: 10.2210/pdb1lqf/pdb
PDB entry 1lqf coloured by chain, front view.
PDB entry 1lqf coloured by chain, side view.
PDB entry 1lqf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of PTP-1B in complex with a peptide inhibitor reveals an alternative binding mode for bisphosphonates.
Asante-Appiah E, Patel S, Dufresne C, Roy P, Wang Q, Patel V, Friesen RW, Ramachandran C, Becker JW, Leblanc Y, Kennedy BP, Scapin G
Biochemistry 41 9043-51 (2002)
PMID: 12119018

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 295 amino acids
Theoretical weight: 34.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P18031 (Residues: 1-283; Coverage: 65%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand BGD 4 x BGD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2
Unit cell:
a: 186.866Å b: 154.421Å c: 64.598Å
α: 90° β: 94.56° γ: 90°
R-values:
R R work R free
0.231 0.228 0.286
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

PTP1B: from the sidelines to the front lines!
Tonks NK. (2003)
5 more

5 mentions without citation

Knowledge-based characterization of similarity relationships in the human protein-tyrosine phosphatase family for rational inhibitor design.
Vidović et al. (2009)
4 more