› 1y9o

Solution NMR

1H NMR Structure of Acylphosphatase from the hyperthermophile Sulfolobus Solfataricus

Released:
DOI: 10.2210/pdb1y9o/pdb
PDB entry 1y9o coloured by chain, ensemble of 20 models, front view.
PDB entry 1y9o coloured by chain, ensemble of 20 models, side view.
PDB entry 1y9o coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus.
Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P
Proteins 62 64-79 (2006)
PMID: 16287076

Function and Biology Details

Reaction catalysed: 
An acylphosphate + H(2)O = a carboxylate + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189083 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acylphosphatase Chain: A
Molecule details ›
Chain: A
Length: 103 amino acids
Theoretical weight: 11.8 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97ZL0 (Residues: 1-101; Coverage: 100%)
Gene names: SSO0887, acyP
Sequence domains: Acylphosphatase
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: restrained minimization
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Protein dynamism and evolvability.
Tokuriki et al. (2009)
1 more

2 mentions without citation

Intrinsically semi-disordered state and its role in induced folding and protein aggregation.
Zhang et al. (2013)
1 more