Structure analysis

Crystal structure of HA17-HA33-Lactulose

X-ray diffraction
2.38Å resolution
Source organism: Clostridium botulinum
Assembly composition:
hetero trimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 31243.6 Å2
Buried surface area: 5077.01 Å2
Dissociation area: 1,083.59 Å2
Dissociation energy (ΔGdiss): 5.01 kcal/mol
Dissociation entropy (TΔSdiss): 12.23 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-175079

Macromolecules

Chains: A, B
Length: 296 amino acids
Theoretical weight: 34.08 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45871 (Residues: 2-293; Coverage: 100%)
Gene names: HA, HA-33, ha33, ha34
Pfam: Ricin-type beta-trefoil lectin domain-like
InterPro:
CATH: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

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Chain: C
Length: 147 amino acids
Theoretical weight: 17.07 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45878 (Residues: 2-146; Coverage: 99%)
Gene names: EXM69_13435, HA, HA-17, ha17
Pfam: Clostridium botulinum HA-17 domain
InterPro:
CATH: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

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