› 2esl

X-ray diffraction
1.9Å resolution

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

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
hetero dodecamer
hetero hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-155359 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase C Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 190 amino acids
Theoretical weight: 20.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P45877 (Residues: 24-212; Coverage: 89%)
Gene names: CYPC, PPIC
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
CYCLOSPORIN A Chains: I, J, K, L, M, N
Molecule details ›
Chains: I, J, K, L, M, N
Length: 11 amino acids
Theoretical weight: 1.22 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand CA 3 x CA
Ligand ZN 2 x ZN
Ligand SO4 6 x SO4
6 modified residues:
Ligand DAL 6 x DAL
Ligand MLE 24 x MLE
Ligand MVA 6 x MVA
Ligand BMT 6 x BMT
Ligand ABA 6 x ABA
Ligand SAR 6 x SAR

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P212121
Unit cell:
a: 72.203Å b: 123.802Å c: 135.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.225
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

37 review citations

Host Factors in Coronavirus Replication.
de Wilde et al. (2018)
36 more

7 mentions without citation

Current update on theranostic roles of cyclophilin A in kidney diseases.
Hadpech et al. (2022)
6 more