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4qd4

X-ray diffraction
1.8Å resolution

Structure of ADC-68, a Novel Carbapenem-Hydrolyzing Class C Extended-Spectrum -Lactamase from Acinetobacter baumannii

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
a beta-lactam + H2O = a substituted beta-amino acid.
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 361 amino acids
Theoretical weight: 40.69 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli
UniProt:
  • Canonical: R4NH29 (Residues: 24-383; Coverage: 100%)
Gene name: blaADC-68
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P212121
Unit cell:
a: 56.393Å b: 71.006Å c: 179.473Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.236
Expression system: Escherichia coli