Structure analysis

Crystal structure of the WbkC N-formyltransferase (F142A variant) from Brucella melitensis

X-ray diffraction
2.2Å resolution
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo dimer
Accessible surface area: 21842.14 Å2
Buried surface area: 5586.86 Å2
Dissociation area: 1,549.89 Å2
Dissociation energy (ΔGdiss): 12.45 kcal/mol
Dissociation entropy (TΔSdiss): 13.48 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-123755
Assembly 2 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 22268.93 Å2
Buried surface area: 5870.91 Å2
Dissociation area: 1,508.04 Å2
Dissociation energy (ΔGdiss): 16.74 kcal/mol
Dissociation entropy (TΔSdiss): 13.51 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-123755

Macromolecules

Chains: A, B, C, D
Length: 261 amino acids
Theoretical weight: 29.24 KDa
Source organism: Brucella melitensis bv. 1 str. 16M
Expression system: Escherichia coli
UniProt:
  • Canonical: F8WJP6 (Residues: 1-259; Coverage: 100%)
Gene names: BAWG_0804, BMEI1418, wbkC
Pfam: Formyl transferase
InterPro:

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