› 2dxp

X-ray diffraction
2.1Å resolution

Crystal structure of the complex of the archaeal sulfolobus PTP-fold phosphatase with phosphopeptides A-(p)Y-R

Released:
DOI: 10.2210/pdb2dxp/pdb
PDB entry 2dxp coloured by chain, front view.
PDB entry 2dxp coloured by chain, side view.
PDB entry 2dxp 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-162676 (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
A(PTR)R Chain: B
Molecule details ›
Chain: B
Length: 3 amino acids
Theoretical weight: 489 Da
Source organism: Saccharolobus solfataricus
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 81.539Å b: 58.232Å c: 36.475Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.252
Expression systems:
  • Escherichia coli BL21
  • Not provided

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Citations

4 review citations

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