Structure analysis

15K X-ray ligand free: Exploring the Mechanism of beta-Lactam Ring Protonation in the Class A beta-lactamase Acylation Mechanism Using Neutron and X-ray Crystallography

X-ray diffraction
1.2Å resolution
Source organism: Escherichia coli
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule


Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 11000 Å2
Buried surface area: 850 Å2
Dissociation area: 50 Å2
Dissociation energy (ΔGdiss): 6 kcal/mol
Dissociation entropy (TΔSdiss): 1 kcal/mol
Interface energy (ΔGint): -64 kcal/mol
Symmetry number: 1


Chain: A
Length: 262 amino acids
Theoretical weight: 28.12 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: E1ANH6 (Residues: 30-291; Coverage: 100%)
Gene name: bla
Pfam: Beta-lactamase enzyme family
CATH: DD-peptidase/beta-lactamase superfamily

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