5a93

Hybrid

293K Joint X-ray Neutron with Cefotaxime: EXPLORING THE MECHANISM OF BETA-LACTAM RING PROTONATION IN THE CLASS A BETA-LACTAMASE ACYLATION MECHANISM USING NEUTRON AND X-RAY CRYSTALLOGRAPHY

Released:

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase CTX-M-97 Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 28.12 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: E1ANH6 (Residues: 30-291; Coverage: 100%)
Gene name: bla
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Experimental Method: Neutron Diffraction, X-ray diffraction
Spacegroup: P3221
Unit cell:
a: 73.315Å b: 73.315Å c: 98.87Å α: 90° β: 90° γ: 120°
R-values:
R R work R free 0.134 0.217 0.156
Expression system: Escherichia coli