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The Sanglifehrin-Cyclophilin Interaction: Degradation Work, Synthetic Macrocyclic Analogues, X-ray Crystal Structure and Binding Data

X-ray diffraction
2.1Å resolution
PDB entry 1nmk coloured by chain, front view.
PDB entry 1nmk coloured by chain, side view.
PDB entry 1nmk coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Peptidyl-prolyl cis-trans isomerase A
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Multimeric state: monomeric
Accessible surface area: 7962.61 Å2
Buried surface area: 906.66 Å2
Dissociation area: 453.33 Å2
Dissociation energy (ΔGdiss): -3.16 kcal/mol
Dissociation entropy (TΔSdiss): 6.19 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-158766
Assembly 2
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Assembly Name: Peptidyl-prolyl cis-trans isomerase A
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Multimeric state: monomeric
Accessible surface area: 7836.04 Å2
Buried surface area: 912.7 Å2
Dissociation area: 456.35 Å2
Dissociation energy (ΔGdiss): -3.44 kcal/mol
Dissociation entropy (TΔSdiss): 6.18 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-158766

Macromolecules

Peptidyl-prolyl cis-trans isomerase A
Chains: A, B
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli str. K-12 substr. W3110
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)
Peptidyl-prolyl cis-trans isomerase A in PDB entry 1nmk, assembly 1, front view.
Peptidyl-prolyl cis-trans isomerase A in PDB entry 1nmk, assembly 1, side view.
Peptidyl-prolyl cis-trans isomerase A in PDB entry 1nmk, assembly 1, top view.
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