› 2hdq

X-ray diffraction
2.1Å resolution

AmpC beta-lactamase in complex with 2-carboxythiophene

Released:
DOI: 10.2210/pdb2hdq/pdb
PDB entry 2hdq coloured by chain, front view.
PDB entry 2hdq coloured by chain, side view.
PDB entry 2hdq coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Deconstructing fragment-based inhibitor discovery.
Babaoglu K, Shoichet BK
Nat Chem Biol 2 720-3 (2006)
PMID: 17072304

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 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 C21 12 x C21
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 119.434Å b: 74.781Å c: 98.281Å
α: 90° β: 116.14° γ: 90°
R-values:
R R work R free
0.183 0.183 0.227
Expression system: Escherichia coli

Quick links

Citations

18 review citations

The rise of fragment-based drug discovery.
Murray et al. (2009)
17 more

2 mentions without citation

Ellagic Acid, Kaempferol, and Quercetin from Acacia nilotica: Promising Combined Drug With Multiple Mechanisms of Action.
Al-Nour et al. (2019)
1 more