› 2hc1

X-ray diffraction
1.3Å resolution

Engineered catalytic domain of protein tyrosine phosphatase HPTPbeta.

Released:
DOI: 10.2210/pdb2hc1/pdb
PDB entry 2hc1 coloured by chain, front view.
PDB entry 2hc1 coloured by chain, side view.
PDB entry 2hc1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Engineering the catalytic domain of human protein tyrosine phosphatase beta for structure-based drug discovery.
Evdokimov AG, Pokross M, Walter R, Mekel M, Cox B, Li C, Bechard R, Genbauffe F, Andrews R, Diven C, Howard B, Rastogi V, Gray J, Maier M, Peters KG
Acta Crystallogr D Biol Crystallogr 62 1435-45 (2006)
PMID: 17139078

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-149972 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor-type tyrosine-protein phosphatase beta Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 33.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23467 (Residues: 1676-1970; Coverage: 15%)
Gene names: PTPB, PTPRB
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand ACT 1 x ACT
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 39.06Å b: 70.714Å c: 118.455Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.136 0.134 0.179
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Protein tyrosine phosphatases: structure-function relationships.
Tabernero et al. (2008)
1 more

2 mentions without citation

Using iterative fragment assembly and progressive sequence truncation to facilitate phasing and crystal structure determination of distantly related proteins.
Wang et al. (2016)
1 more