› 1cwf

X-ray diffraction
1.86Å resolution

HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL CYCLOSPORIN

Released:
DOI: 10.2210/pdb1cwf/pdb
PDB entry 1cwf coloured by chain, front view.
PDB entry 1cwf coloured by chain, side view.
PDB entry 1cwf coloured by chain, top view.
Source organisms:
Primary publication:
X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A.
Kallen J, Mikol V, Taylor P, Walkinshaw MD
J Mol Biol 283 435-49 (1998)
PMID: 9769216

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158778 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
CYCLOSPORIN D Chain: C
Molecule details ›
Chain: C
Length: 11 amino acids
Theoretical weight: 1.23 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided

Ligands and Environments

No bound ligands
5 modified residues:
Ligand DAL 1 x DAL
Ligand MLE 4 x MLE
Ligand MVA 1 x MVA
Ligand BMT 1 x BMT
Ligand SAR 1 x SAR

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 36.4Å b: 61.42Å c: 72.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 not available
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Enzymes that catalyse the restructuring of proteins.
Schiene et al. (2000)
3 more