1c5f

X-ray diffraction
2.47Å resolution

CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A

Released:

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase 1 Chains: A, C, E, G, I, K, M, O
Molecule details ›
Chains: A, C, E, G, I, K, M, O
Length: 177 amino acids
Theoretical weight: 19.5 KDa
Source organism: Brugia malayi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27450 (Residues: 1-177; Coverage: 21%)
Gene name: CYP-1
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
CYCLOSPORIN A Chains: B, D, F, H, J, L, N, P
Molecule details ›
Chains: B, D, F, H, J, L, N, P
Length: 11 amino acids
Theoretical weight: 1.22 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided

Ligands and Environments

No bound ligands

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 62Å b: 100.16Å c: 133.92Å
α: 90° β: 93.75° γ: 90°
R-values:
R R work R free
0.201 0.201 0.249
Expression systems:
  • Escherichia coli
  • Not provided