› 3o4s

X-ray diffraction
1.9Å resolution

Crystal Structure of HePTP with a Closed WPD Loop and an Ordered E-Loop

Released:
DOI: 10.2210/pdb3o4s/pdb
PDB entry 3o4s coloured by chain, front view.
PDB entry 3o4s coloured by chain, side view.
PDB entry 3o4s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Visualizing active-site dynamics in single crystals of HePTP: opening of the WPD loop involves coordinated movement of the E loop.
Critton DA, Tautz L, Page R
J Mol Biol 405 619-29 (2011)
PMID: 21094165

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-152862 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 7 Chain: A
Molecule details ›
Chain: A
Length: 308 amino acids
Theoretical weight: 35.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35236 (Residues: 65-360; Coverage: 82%)
Gene name: PTPN7
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand SO4 6 x SO4
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: C2
Unit cell:
a: 117.795Å b: 39.13Å c: 83.441Å
α: 90° β: 124.29° γ: 90°
R-values:
R R work R free
0.164 0.162 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Protein tyrosine phosphatases: structure, function, and implication in human disease.
Tautz et al. (2013)
2 more

1 mention without citation

Visualizing active-site dynamics in single crystals of HePTP: opening of the WPD loop involves coordinated movement of the E loop.
Critton et al. (2011)