› 2k7k

Solution NMR

Human Acylphosphatase (AcPh) common type

Released:
DOI: 10.2210/pdb2k7k/pdb
PDB entry 2k7k coloured by chain, ensemble of 20 models, front view.
PDB entry 2k7k coloured by chain, ensemble of 20 models, side view.
PDB entry 2k7k coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Rational stabilization of enzymes by computational redesign of surface charge-charge interactions.
Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI
Proc Natl Acad Sci U S A 106 2601-6 (2009)
PMID: 19196981

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-139497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acylphosphatase-1 Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 11.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07311 (Residues: 2-99; Coverage: 99%)
Gene names: ACYP1, ACYPE
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: DGSA-distance geometry simulated annealing, torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Stability of protein pharmaceuticals: an update.
Manning et al. (2010)
15 more

1 mention without citation

Rational stabilization of enzymes by computational redesign of surface charge-charge interactions.
Gribenko et al. (2009)