Structure analysis

Crystal structure of the T150A mutant of Malonamidase E2 from Bradyrhizobium japonicum

X-ray diffraction
1.9Å resolution
Source organism: Bradyrhizobium japonicum
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: 27213.54 Å2
Buried surface area: 3025.58 Å2
Dissociation area: 1,512.79 Å2
Dissociation energy (ΔGdiss): -0.12 kcal/mol
Dissociation entropy (TΔSdiss): 14.16 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-195661

Macromolecules

Chains: A, B
Length: 414 amino acids
Theoretical weight: 43.71 KDa
Source organism: Bradyrhizobium japonicum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ZIV5 (Residues: 1-414; Coverage: 100%)
Pfam: Amidase
InterPro:
CATH: Amidase signature (AS) domain
SCOP: Amidase signature (AS) enzymes

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