› 1c3b

X-ray diffraction
2.25Å resolution

AMPC BETA-LACTAMASE FROM E. COLI COMPLEXED WITH INHIBITOR, BENZO(B)THIOPHENE-2-BORONIC ACID (BZB)

Released:
DOI: 10.2210/pdb1c3b/pdb
PDB entry 1c3b coloured by chain, front view.
PDB entry 1c3b coloured by chain, side view.
PDB entry 1c3b coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase.
Powers RA, Bl��zquez J, Weston GS, Morosini MI, Baquero F, Shoichet BK
Protein Sci. 8 2330-7 (1999)
PMID: 10595535

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133600 (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 BZB 2 x BZB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 118.859Å b: 78.012Å c: 98.962Å
α: 90° β: 116.066° γ: 90°
R-values:
R R work R free
0.167 0.167 0.224
Expression system: Escherichia coli

Quick links

Citations

12 review citations

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

3 mentions without citation

Re-examining the role of Lys67 in class C beta-lactamase catalysis.
Chen et al. (2009)
2 more