› 2gv1

Solution NMR

NMR solution structure of the Acylphosphatase from Eschaerichia Coli

Released:
DOI: 10.2210/pdb2gv1/pdb
PDB entry 2gv1 coloured by chain, ensemble of 20 models, front view.
PDB entry 2gv1 coloured by chain, ensemble of 20 models, side view.
PDB entry 2gv1 coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
NMR solution structure of the acylphosphatase from Escherichia coli.
Pagano K, Ramazzotti M, Viglino P, Esposito G, Degl'Innocenti D, Taddei N, Corazza A
J Biomol NMR 36 199-204 (2006)
PMID: 17021943

Function and Biology Details

Reaction catalysed: 
An acylphosphate + H(2)O = a carboxylate + 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-142017 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acylphosphatase Chain: A
Molecule details ›
Chain: A
Length: 92 amino acids
Theoretical weight: 10.31 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AB65 (Residues: 1-92; Coverage: 100%)
Gene names: JW5131, b0968, yccX
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: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Methods for structural characterization of prefibrillar intermediates and amyloid fibrils.
Langkilde et al. (2009)
1 more

1 mention without citation

Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?
Sacquin-Mora S. (2015)