Structure analysis

Crystal Structure of N-terminal G-domain of EngA from Bacillus subtilis

X-ray diffraction
1.5Å resolution
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: monomeric
Accessible surface area: 7200 Å2
Buried surface area: 1200 Å2
Dissociation area: 100 Å2
Dissociation energy (ΔGdiss): 13 kcal/mol
Dissociation entropy (TΔSdiss): -1 kcal/mol
Interface energy (ΔGint): -153 kcal/mol
Symmetry number: 1
Assembly 2
Download    3D Visualisation
Multimeric state: monomeric

Binding statistics and energies are not available for this assembly

Macromolecules

Chains: A, B
Length: 162 amino acids
Theoretical weight: 17.78 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P50743 (Residues: 2-163; Coverage: 37%)
Gene names: BSU22840, der, engA, yphC
Pfam: 50S ribosome-binding GTPase
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases

Search similar proteins