› 3iwo

X-ray diffraction
1.9Å resolution

X-ray crystal structure of the extended-spectrum AmpC Y221G mutant beta-lactamase at 1.90 Angstrom resolution

Released:
DOI: 10.2210/pdb3iwo/pdb
PDB entry 3iwo coloured by chain, front view.
PDB entry 3iwo coloured by chain, side view.
PDB entry 3iwo 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
Macromolecules (2 distinct):
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 39.48 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

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
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: 117.717Å b: 76.789Å c: 98.693Å
α: 90° β: 116.62° γ: 90°
R-values:
R R work R free
0.159 0.157 0.197
Expression system: Escherichia coli

Quick links

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)