› 2rcx

X-ray diffraction
2Å resolution

AmpC Beta-lactamase in complex with (1R)-1-(2-Thiophen-2-yl-acetylamino)-1-(3-(2-carboxyvinyl)-phenyl) methylboronic acid

Released:
DOI: 10.2210/pdb2rcx/pdb
PDB entry 2rcx coloured by chain, front view.
PDB entry 2rcx coloured by chain, side view.
PDB entry 2rcx coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure-based optimization of cephalothin-analogue boronic acids as beta-lactamase inhibitors.
Morandi S, Morandi F, Caselli E, Shoichet BK, Prati F
Bioorg Med Chem 16 1195-205 (2008)
PMID: 17997318

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

2 bound ligands:
Ligand SM4 2 x SM4
Ligand PO4 2 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: 118.378Å b: 76.937Å c: 97.254Å
α: 90° β: 115.87° γ: 90°
R-values:
R R work R free
0.178 0.176 0.219
Expression system: Escherichia coli K-12

Quick links

Citations

12 review citations

New β-lactamase inhibitors: a therapeutic renaissance in an MDR world.
Drawz et al. (2014)
11 more

1 mention without citation

Structure-based optimization of cephalothin-analogue boronic acids as beta-lactamase inhibitors.
Morandi et al. (2008)