› 1wch

X-ray diffraction
1.85Å resolution

Crystal structure of PTPL1 human tyrosine phosphatase mutated in colorectal cancer - evidence for a second phosphotyrosine substrate recognition pocket

Released:
DOI: 10.2210/pdb1wch/pdb
PDB entry 1wch coloured by chain, front view.
PDB entry 1wch coloured by chain, side view.
PDB entry 1wch coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket.
Villa F, Deak M, Bloomberg GB, Alessi DR, van Aalten DM
J Biol Chem 280 8180-7 (2005)
PMID: 15611135

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-171438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 13 Chain: A
Molecule details ›
Chain: A
Length: 315 amino acids
Theoretical weight: 36.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q12923 (Residues: 2163-2477; Coverage: 13%)
Gene names: PNP1, PTP1E, PTPL1, PTPN13
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2
Unit cell:
a: 99.707Å b: 59.193Å c: 66.075Å
α: 90° β: 113.05° γ: 90°
R-values:
R R work R free
0.177 0.177 0.204
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Protein tyrosine phosphatases as potential therapeutic targets.
He et al. (2014)
4 more

4 mentions without citation

The role of E. coli Nus-factors in transcription regulation and transcription:translation coupling: From structure to mechanism.
Burmann et al. (2011)
3 more