› 3iwi

X-ray diffraction
1.64Å resolution

X-ray crystal structure of the extended-spectrum AmpC omega loop insertion (H210AAA) mutant beta-lactamase at 1.64 Angstrom resolution

Released:
DOI: 10.2210/pdb3iwi/pdb
PDB entry 3iwi coloured by chain, front view.
PDB entry 3iwi coloured by chain, side view.
PDB entry 3iwi 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

Assembly composition:
monomeric (preferred)
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: 361 amino acids
Theoretical weight: 39.8 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00811 (Residues: 20-226, 227-377; 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 PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 117.582Å b: 77.926Å c: 98.05Å
α: 90° β: 115.96° γ: 90°
R-values:
R R work R free
0.171 0.17 0.196
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

2 mentions without citation

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