Structure analysis

Crystal structure of N(1-260) of human FKBP52

X-ray diffraction
1.9Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 12954.57 Å2
Buried surface area: 1174.62 Å2
Dissociation area: 123.23 Å2
Dissociation energy (ΔGdiss): -3.5 kcal/mol
Dissociation entropy (TΔSdiss): 0.08 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-169761

Macromolecules

Chain: A
Length: 280 amino acids
Theoretical weight: 31.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02790 (Residues: 2-260; Coverage: 56%)
Gene names: FKBP4, FKBP52
Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase
InterPro:
CATH: Chitinase A; domain 3
SCOP: FKBP immunophilin/proline isomerase

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