› 5a91

X-ray diffraction
1.2Å resolution

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

Released:
DOI: 10.2210/pdb5a91/pdb
PDB entry 5a91 coloured by chain, front view.
PDB entry 5a91 coloured by chain, side view.
PDB entry 5a91 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Exploring the Mechanism of β-Lactam Ring Protonation in the Class A β-lactamase Acylation Mechanism Using Neutron and X-ray Crystallography.
Vandavasi VG, Weiss KL, Cooper JB, Erskine PT, Tomanicek SJ, Ostermann A, Schrader TE, Ginell SL, Coates L
J Med Chem 59 474-9 (2016)
PMID: 26630115

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122738 (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:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3221
Unit cell:
a: 72.398Å b: 72.398Å c: 97.198Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.13 0.129 0.15
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
Bahr et al. (2021)
2 more

1 mention without citation

β-Lactamase of Mycobacterium tuberculosis Shows Dynamics in the Active Site That Increase upon Inhibitor Binding.
Elings et al. (2020)