› 2i6o

X-ray diffraction
1.9Å resolution

Crystal structure of the complex of the archaeal sulfolobus PTP-fold phosphatase with phosphopeptides N-G-(p)Y-K-N

Released:
DOI: 10.2210/pdb2i6o/pdb
PDB entry 2i6o coloured by chain, front view.
PDB entry 2i6o coloured by chain, side view.
PDB entry 2i6o 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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162746 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein phosphatase Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 18.42 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
NK(PTR)GN Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 676 Da
Source organism: Saccharolobus solfataricus
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand PG4 2 x PG4
Ligand CA 1 x CA
Ligand IMD 3 x IMD
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 80.979Å b: 58.399Å c: 36.435Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.227
Expression systems:
  • Escherichia coli BL21
  • Not provided

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

1 mention without citation

Structural basis for the glucan phosphatase activity of Starch Excess4.
Vander Kooi et al. (2010)