› 2ffy

X-ray diffraction
1.07Å resolution

AmpC beta-lactamase N289A mutant in complex with a boronic acid deacylation transition state analog compound SM3

Released:
DOI: 10.2210/pdb2ffy/pdb
Model geometry
Fit model/data
PDB entry 2ffy coloured by chain, front view.
PDB entry 2ffy coloured by chain, side view.
PDB entry 2ffy coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The deacylation mechanism of AmpC beta-lactamase at ultrahigh resolution.
Chen Y, Minasov G, Roth TA, Prati F, Shoichet BK
J Am Chem Soc 128 2970-6 (2006)
PMID: 16506777

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: 39.54 KDa
Source organism: Escherichia coli
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

3 bound ligands:
Ligand K 2 x K
Ligand SM3 2 x SM3
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: C2
Unit cell:
a: 118.84Å b: 76.063Å c: 97.898Å
α: 90° β: 115.85° γ: 90°
R-values:
R R work R free
0.133 0.133 0.164
Expression system: Escherichia coli

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Citations

15 review citations

AmpC beta-lactamases.
Jacoby GA. (2009)
14 more

2 mentions without citation

The deacylation mechanism of AmpC beta-lactamase at ultrahigh resolution.
Chen et al. (2006)
1 more