› 3fkw

X-ray diffraction
1.5Å resolution

AmpC K67R mutant apo structure

Released:
DOI: 10.2210/pdb3fkw/pdb
PDB entry 3fkw coloured by chain, front view.
PDB entry 3fkw coloured by chain, side view.
PDB entry 3fkw coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Re-examining the role of Lys67 in class C beta-lactamase catalysis.
Chen Y, McReynolds A, Shoichet BK
Protein Sci 18 662-9 (2009)
PMID: 19241376

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 analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
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: 39.62 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 118.348Å b: 76.564Å c: 97.702Å
α: 90° β: 115.82° γ: 90°
R-values:
R R work R free
0.167 0.166 0.199
Expression system: Escherichia coli

Quick links

Citations

6 review citations

β-Lactamases and β-Lactamase Inhibitors in the 21st Century.
Tooke et al. (2019)
5 more

1 mention without citation

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