› 1cwh

X-ray diffraction
1.86Å resolution

HUMAN CYCLOPHILIN A COMPLEXED WITH 3-D-SER CYCLOSPORIN

Released:
DOI: 10.2210/pdb1cwh/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1cwh coloured by chain, front view.
PDB entry 1cwh coloured by chain, side view.
PDB entry 1cwh 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-158779 (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 A Chain: C
Molecule details ›
Chain: C
Length: 11 amino acids
Theoretical weight: 1.25 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided

Ligands and Environments

No bound ligands
6 modified residues:
Ligand DAL 1 x DAL
Ligand MLE 4 x MLE
Ligand MVA 1 x MVA
Ligand BMT 1 x BMT
Ligand ABA 1 x ABA
Ligand DSE 1 x DSE

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P21212
Unit cell:
a: 62.9Å b: 65.3Å c: 40.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 not available
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Versatile TPR domains accommodate different modes of target protein recognition and function.
Allan et al. (2011)
3 more

1 mention without citation

Investigating the Release of a Hydrophobic Peptide from Matrices of Biodegradable Polymers: An Integrated Method Approach.
Gubskaya et al. (2013)