Entry | Database: PDB / ID: 4y0o |
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Title | Crystal structure of OXA-58, a carbapenem hydrolyzing Class D beta-lactamase from Acinetobacter baumanii. |
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Components | Beta-lactamase |
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Keywords | HYDROLASE / OXA-58 / A. baumannii / carbapenemase / beta lactamase |
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Function / homology | Function and homology information
penicillin binding / antibiotic catabolic process / cell wall organization / beta-lactamase activity / beta-lactamase / response to antibioticSimilarity search - Function Beta-lactamase, class-D active site / Beta-lactamase class-D active site. / Penicillin-binding protein, transpeptidase / Penicillin binding protein transpeptidase domain / Beta-lactamase / DD-peptidase/beta-lactamase superfamily / Beta-lactamase/transpeptidase-like / Prokaryotic membrane lipoprotein lipid attachment site profile. / 3-Layer(aba) Sandwich / Alpha BetaSimilarity search - Domain/homology |
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Biological species | Acinetobacter baumannii (bacteria) |
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Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.37 Å |
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Authors | Pratap, S. / Katiki, M. / Gill, P. / Golemi-Kotra, D. / Kumar, P. |
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Citation | Journal: Antimicrob.Agents Chemother. / Year: 2015 Title: Active-Site Plasticity Is Essential to Carbapenem Hydrolysis by OXA-58 Class D beta-Lactamase of Acinetobacter baumannii. Authors: Pratap, S. / Katiki, M. / Gill, P. / Kumar, P. / Golemi-Kotra, D. |
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History | Deposition | Feb 6, 2015 | Deposition site: RCSB / Processing site: PDBJ |
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Revision 1.0 | Jan 13, 2016 | Provider: repository / Type: Initial release |
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