› 1l0g

X-ray diffraction
1.5Å resolution

X-ray Crystal Structure of AmpC S64G Mutant beta-Lactamase

Released:
DOI: 10.2210/pdb1l0g/pdb
PDB entry 1l0g coloured by chain, front view.
PDB entry 1l0g coloured by chain, side view.
PDB entry 1l0g coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural bases of stability-function tradeoffs in enzymes.
Beadle BM, Shoichet BK
J Mol Biol 321 285-96 (2002)
PMID: 12144785

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
Macromolecules (2 distinct):
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 39.56 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

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
1 bound ligand:
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: C2
Unit cell:
a: 118.387Å b: 76.329Å c: 97.665Å
α: 90° β: 115.76° γ: 90°
R-values:
R R work R free
0.189 0.189 0.212
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Missense meanderings in sequence space: a biophysical view of protein evolution.
DePristo et al. (2005)
17 more

1 mention without citation

Characterization of anti-leukemia components from Indigo naturalis using comprehensive two-dimensional K562/cell membrane chromatography and in silico target identification.
Wu et al. (2016)