Structure analysis

Structure of the human sterol O-acyltransferase 1 in resting state

Electron Microscopy
3.5Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 39424.41 Å2
Buried surface area: 5504.54 Å2
Dissociation area: 1,894.82 Å2
Dissociation energy (ΔGdiss): 18.57 kcal/mol
Dissociation entropy (TΔSdiss): 14.45 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-152963

Macromolecules

Chains: A, B
Length: 485 amino acids
Theoretical weight: 57.29 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P35610 (Residues: 66-550; Coverage: 88%)
Gene names: ACACT, ACACT1, ACAT, ACAT1, SOAT, SOAT1, STAT
Pfam: MBOAT, membrane-bound O-acyltransferase family
InterPro:

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