› 3ixg

X-ray diffraction
2.14Å resolution

X-ray crystal structure of the extended-spectrum AmpC T70I mutant beta-lactamase with and without benzo(b)thiophene-2-boronic acid bound at 2.14 Angstrom resolution

Released:
DOI: 10.2210/pdb3ixg/pdb
PDB entry 3ixg coloured by chain, front view.
PDB entry 3ixg coloured by chain, side view.
PDB entry 3ixg coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural bases for stability-function tradeoffs in antibiotic resistance.
Thomas VL, McReynolds AC, Shoichet BK
J Mol Biol 396 47-59 (2010)
PMID: 19913034

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-133599 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 39.6 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00811 (Residues: 20-377; Coverage: 100%)
Gene names: JW4111, ampA, ampC, b4150
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand BZB 1 x BZB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 114.162Å b: 77.361Å c: 91.747Å
α: 90° β: 122.12° γ: 90°
R-values:
R R work R free
0.199 0.197 0.245
Expression system: Escherichia coli

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Citations

10 review citations

Evolutionary biochemistry: revealing the historical and physical causes of protein properties.
Harms et al. (2013)
9 more

1 mention without citation

Structural bases for stability-function tradeoffs in antibiotic resistance.
Thomas et al. (2010)