› 4kz5

X-ray diffraction
1.35Å resolution

Crystal structure of AmpC beta-lactamase in complex with fragment 5 (N-{[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]carbonyl}glycine)

Released:
DOI: 10.2210/pdb4kz5/pdb
PDB entry 4kz5 coloured by chain, front view.
PDB entry 4kz5 coloured by chain, side view.
PDB entry 4kz5 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Increasing chemical space coverage by combining empirical and computational fragment screens.
Barelier S, Eidam O, Fish I, Hollander J, Figaroa F, Nachane R, Irwin JJ, Shoichet BK, Siegal G
ACS Chem Biol 9 1528-35 (2014)
PMID: 24807704

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

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 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

2 bound ligands:
Ligand 1U3 2 x 1U3
Ligand PO4 4 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: 118.08Å b: 76.86Å c: 97.71Å
α: 90° β: 116.26° γ: 90°
R-values:
R R work R free
0.136 0.135 0.156
Expression system: Escherichia coli

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Citations

9 review citations

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1 mention without citation

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