Structure analysis

Crystallographic structure of trimeric riboflavin synthase from Brucella abortus

X-ray diffraction
1.9Å resolution
Source organism: Brucella abortus
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: 24026.68 Å2
Buried surface area: 5280.04 Å2
Dissociation area: 1,448.08 Å2
Dissociation energy (ΔGdiss): 18.24 kcal/mol
Dissociation entropy (TΔSdiss): 12.81 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-164477

Macromolecules

Chains: A, B, C
Length: 210 amino acids
Theoretical weight: 23.32 KDa
Source organism: Brucella abortus
Expression system: Escherichia coli BL21(DE3)
InterPro:
CATH: Elongation Factor Tu (Ef-tu); domain 3

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