› 1oca

Solution NMR

HUMAN CYCLOPHILIN A, UNLIGATED, NMR, 20 STRUCTURES

Released:
DOI: 10.2210/pdb1oca/pdb
PDB entry 1oca coloured by chain, ensemble of 20 models, front view.
PDB entry 1oca coloured by chain, ensemble of 20 models, side view.
PDB entry 1oca coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The NMR solution conformation of unligated human cyclophilin A.
Ottiger M, Zerbe O, Güntert P, Wüthrich K
J Mol Biol 272 64-81 (1997)
PMID: 9299338

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase A Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62937 (Residues: 1-165; Coverage: 100%)
Gene names: CYPA, PPIA
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Validation of protein models derived from experiment.
Laskowski et al. (1998)
5 more

14 mentions without citation

Conformer selection and induced fit in flexible backbone protein-protein docking using computational and NMR ensembles.
Chaudhury et al. (2008)
13 more