› 1xgi

X-ray diffraction
1.96Å resolution

AmpC beta-lactamase in complex with 3-(3-nitro-phenylsulfamoyl)-thiophene-2-carboxylic acid

Released:
DOI: 10.2210/pdb1xgi/pdb
PDB entry 1xgi coloured by chain, front view.
PDB entry 1xgi coloured by chain, side view.
PDB entry 1xgi coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure-based optimization of a non-beta-lactam lead results in inhibitors that do not up-regulate beta-lactamase expression in cell culture.
Tondi D, Morandi F, Bonnet R, Costi MP, Shoichet BK
J Am Chem Soc 127 4632-9 (2005)
PMID: 15796528

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 domain:

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: 358 amino acids
Theoretical weight: 39.59 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli K-12
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 NST 1 x NST
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 118.469Å b: 76.279Å c: 97.674Å
α: 90° β: 116.37° γ: 90°
R-values:
R R work R free
0.198 0.198 0.226
Expression system: Escherichia coli K-12

Quick links

Citations

7 review citations

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
6 more

4 mentions without citation

Solvents to Fragments to Drugs: MD Applications in Drug Design.
Defelipe et al. (2018)
3 more