› 2i6m

X-ray diffraction
1.9Å resolution

Crystal structure of the complexes of the archaeal sulfolobus PTP-fold phosphatase with Tungstate

Released:
DOI: 10.2210/pdb2i6m/pdb
PDB entry 2i6m coloured by chain, front view.
PDB entry 2i6m coloured by chain, side view.
PDB entry 2i6m coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes.
Chu HM, Wang AH
Proteins 66 996-1003 (2007)
PMID: 17173287

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188996 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein phosphatase Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 18.43 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q97VZ7 (Residues: 1-161; Coverage: 100%)
Gene name: SSO2453
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand WO4 1 x WO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P41
Unit cell:
a: 72.288Å b: 72.288Å c: 32.518Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.233
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
3 more

2 mentions without citation

New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening.
Kuznetsov et al. (2012)
1 more