Structure analysis

Structure of a carnitinyl-CoA dehydratase from Mycobacterium avium 104

X-ray diffraction
2.2Å resolution
Source organism: Mycobacterium avium 104
Assembly composition:
homo trimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo trimer
Accessible surface area: 27532.11 Å2
Buried surface area: 10017.02 Å2
Dissociation area: 4,292.48 Å2
Dissociation energy (ΔGdiss): 38.46 kcal/mol
Dissociation entropy (TΔSdiss): 27.05 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-101740

Macromolecules

Chains: A, B, C
Length: 267 amino acids
Theoretical weight: 28.16 KDa
Source organism: Mycobacterium avium 104
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H2ZTH2 (Residues: 1-263; Coverage: 100%)
Gene name: MAV_1277
Pfam: Enoyl-CoA hydratase/isomerase
InterPro:
CATH:

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