› 2c7s

X-ray diffraction
1.95Å resolution

Crystal structure of human protein tyrosine phosphatase kappa at 1.95A resolution

Released:
DOI: 10.2210/pdb2c7s/pdb
PDB entry 2c7s coloured by chain, front view.
PDB entry 2c7s coloured by chain, side view.
PDB entry 2c7s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1.
Eswaran J, Debreczeni JE, Longman E, Barr AJ, Knapp S
Protein Sci 15 1500-5 (2006)
PMID: 16672235

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-172239 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor-type tyrosine-protein phosphatase kappa Chain: A
Molecule details ›
Chain: A
Length: 313 amino acids
Theoretical weight: 36.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15262 (Residues: 853-1154; Coverage: 21%)
Gene names: PTPK, PTPRK
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P43212
Unit cell:
a: 91.373Å b: 91.373Å c: 108.415Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.2 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 citation in other articles

Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn.
Lim et al. (2009)
6 more

5 mentions without citation

Protein tyrosine phosphatase PTPRT as a regulator of synaptic formation and neuronal development.
Lee JR. (2015)
4 more