Structure analysis

Crystal structure of cyclophilin from Leishmania donovani ligated with cyclosporin A

X-ray diffraction
2.6Å resolution
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero dimer
Accessible surface area: 7922.66 Å2
Buried surface area: 992.56 Å2
Dissociation area: 496.28 Å2
Dissociation energy (ΔGdiss): 2.82 kcal/mol
Dissociation entropy (TΔSdiss): 7.12 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-163515
Assembly 2 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 8015.18 Å2
Buried surface area: 990.06 Å2
Dissociation area: 495.03 Å2
Dissociation energy (ΔGdiss): 2.31 kcal/mol
Dissociation entropy (TΔSdiss): 7.13 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-163515

Macromolecules

Chains: A, B
Length: 172 amino acids
Theoretical weight: 19.09 KDa
Source organism: Leishmania donovani
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9U9R3 (Residues: 22-187; Coverage: 100%)
Gene name: CYP
Pfam: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
InterPro:
CATH: Cyclophilin-like

Search similar proteins

Chains: C, D
Length: 11 amino acids
Theoretical weight: 1.22 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided

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