› 3k0p

X-ray diffraction
1.65Å resolution

Cryogenic structure of CypA mutant Ser99Thr

Released:
DOI: 10.2210/pdb3k0p/pdb
PDB entry 3k0p coloured by chain, front view.
PDB entry 3k0p coloured by chain, side view.
PDB entry 3k0p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Hidden alternative structures of proline isomerase essential for catalysis.
Fraser JS, Clarkson MW, Degnan SC, Erion R, Kern D, Alber T
Nature 462 669-73 (2009)
PMID: 19956261

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-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: 18.05 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
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P3221
Unit cell:
a: 59.683Å b: 59.683Å c: 94.261Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.15 0.147 0.176
Expression system: Escherichia coli

Quick links

Citations

52 review citations

The ensemble nature of allostery.
Motlagh et al. (2014)
51 more

1 mention without citation

Hidden alternative structures of proline isomerase essential for catalysis.
Fraser et al. (2009)