› 2rmc

X-ray diffraction
1.64Å resolution

Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A

Released:
DOI: 10.2210/pdb2rmc/pdb
PDB entry 2rmc coloured by chain, front view.
PDB entry 2rmc coloured by chain, side view.
PDB entry 2rmc coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A.
Ke H, Zhao Y, Luo F, Weissman I, Friedman J
Proc Natl Acad Sci U S A 90 11850-4 (1993)
PMID: 8265636

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151720 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase C Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 182 amino acids
Theoretical weight: 19.94 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P30412 (Residues: 31-212; Coverage: 86%)
Gene names: Cypc, Ppic
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
CYCLOSPORIN A Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 11 amino acids
Theoretical weight: 1.22 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided

Ligands and Environments

No bound ligands
6 modified residues:
Ligand DAL 4 x DAL
Ligand MLE 16 x MLE
Ligand MVA 4 x MVA
Ligand BMT 4 x BMT
Ligand ABA 4 x ABA
Ligand SAR 4 x SAR

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 60.3Å b: 74Å c: 97.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 not available
Expression system: Not provided

Quick links

Citations

6 review citations

The cyclophilins.
Wang et al. (2005)
5 more

4 mentions without citation

Dead-end elimination with perturbations (DEEPer): a provable protein design algorithm with continuous sidechain and backbone flexibility.
Hallen et al. (2013)
3 more