Structure analysis

The crystal structure of the carbapenemase OXA-24 reveals new insights into the mechanism of carbapenem-hydrolysis

X-ray diffraction
2.5Å resolution
Source organism: Acinetobacter baumannii
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 11092.62 Å2
Buried surface area: 210.39 Å2
Dissociation area: 105.19 Å2
Dissociation energy (ΔGdiss): 18.58 kcal/mol
Dissociation entropy (TΔSdiss): 0.61 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-186001

Macromolecules

Chain: A
Length: 244 amino acids
Theoretical weight: 27.54 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8RLA6 (Residues: 32-275; Coverage: 96%)
Gene names: APD33_00525, MKP18_004229, MKP18_004230, MKP18_004396, MKP18_004397, bla-OXA-40, blaOXA-24, blaOXA-33, blaOXA-40, oxa-24, oxa40
Pfam: Penicillin binding protein transpeptidase domain
InterPro:
CATH: DD-peptidase/beta-lactamase superfamily

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