› 1pty

X-ray diffraction
1.85Å resolution

CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH TWO PHOSPHOTYROSINE MOLECULES

Released:
DOI: 10.2210/pdb1pty/pdb
PDB entry 1pty coloured by chain, front view.
PDB entry 1pty coloured by chain, side view.
PDB entry 1pty coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design.
Puius YA, Zhao Y, Sullivan M, Lawrence DS, Almo SC, Zhang ZY
Proc Natl Acad Sci U S A 94 13420-5 (1997)
PMID: 9391040

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: 321 amino acids
Theoretical weight: 37.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P18031 (Residues: 1-321; Coverage: 74%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand PTR 2 x PTR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P3121
Unit cell:
a: 87.909Å b: 87.909Å c: 103.822Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.181 not available
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

42 review citations

Protein tyrosine phosphatases in the human genome.
Alonso et al. (2004)
41 more

20 mentions without citation

Molecular docking: a powerful approach for structure-based drug discovery.
Meng et al. (2011)
19 more