› 2n0t

Solution NMR

Structural ensemble of the enzyme cyclophilin reveals an orchestrated mode of action at atomic resolution

Released:
DOI: 10.2210/pdb2n0t/pdb
PDB entry 2n0t coloured by chain, ensemble of 40 models, front view.
PDB entry 2n0t coloured by chain, ensemble of 40 models, side view.
PDB entry 2n0t coloured by chain, ensemble of 40 models, top view.
Source organism: Homo sapiens
Primary publication:
A Structural Ensemble for the Enzyme Cyclophilin Reveals an Orchestrated Mode of Action at Atomic Resolution.
Chi CN, Vögeli B, Bibow S, Strotz D, Orts J, Güntert P, Riek R
Angew Chem Int Ed Engl 54 11657-61 (2015)
PMID: 26265096

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-549123 (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
Chemical shift assignment: 83%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The Exact Nuclear Overhauser Enhancement: Recent Advances.
Nichols et al. (2017)
1 more

2 mentions without citation

Dynamic design: manipulation of millisecond timescale motions on the energy landscape of cyclophilin A.
Juárez-Jiménez et al. (2020)
1 more