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TitleHis224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency in the Metallo-Beta-Lactamase Vim-7.
Journal, issue, pagesAntimicrob. Agents Chemother., Vol. 58, Page 4826-, Year 2014
Publish dateMay 5, 2014 (structure data deposition date)
AuthorsLeiros, H.-K.S. / Skagseth, S. / Edvardsen, K.S.W. / Lorentzen, M.S. / Bjerga, G.E.K. / Leiros, I. / Samuelsen, O.
External linksAntimicrob. Agents Chemother. / PubMed:24913158
MethodsX-ray diffraction
Resolution1.25 - 1.8 Å
Structure data

PDB-4d1t:
High resolution structure of native tVIM-7 from Pseudomonas aeruginosa
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

PDB-4d1u:
A D120A mutant of VIM-7 from Pseudomonas aeruginosa
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-4d1v:
A F218Y mutant of VIM-7 from Pseudomonas aeruginosa
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-4d1w:
A H224Y mutant for VIM-7 from Pseudomonas aeruginosa
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • pseudomonas aeruginosa (bacteria)
KeywordsHYDROLASE / RESIDUE DETERMINANTS / LIGAND INTERACTION

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