Structure analysis

Crystal Structure of human calcineurin complexed with cyclosporin A and human cyclophilin

X-ray diffraction
3.1Å resolution
Assembly composition:
Non-polymer only tetramer (preferred)
Entry contents: 4 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: Non-polymer only tetramer
Accessible surface area: 28800 Å2
Buried surface area: 7400 Å2
Dissociation area: 1,000 Å2
Dissociation energy (ΔGdiss): 15 kcal/mol
Dissociation entropy (TΔSdiss): 7 kcal/mol
Interface energy (ΔGint): -91 kcal/mol
Symmetry number: 1

Macromolecules

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Chain: B
Length: 170 amino acids
Theoretical weight: 19.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P63098 (Residues: 1-170; Coverage: 100%)
Gene names: CNA2, CNB, PPP3R1
Pfam:
InterPro:
CATH: EF-hand
SCOP: Calmodulin-like

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Chain: C
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
Pfam: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
InterPro:
CATH: Cyclophilin-like
SCOP: Cyclophilin (peptidylprolyl isomerase)

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

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