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-Structure paper
Title | Natural variants modify Klebsiella pneumoniae carbapenemase (KPC) acyl-enzyme conformational dynamics to extend antibiotic resistance. |
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Journal, issue, pages | J. Biol. Chem., Vol. 296, Page 100126-100126, Year 2020 |
Publish date | May 14, 2020 (structure data deposition date) |
Authors | Tooke, C.L. / Hinchliffe, P. / Bonomo, R.A. / Schofield, C.J. / Mulholland, A.J. / Spencer, J. |
External links | J. Biol. Chem. / PubMed:33257320 |
Methods | X-ray diffraction |
Resolution | 1.24 - 1.4 Å |
Structure data | PDB-6z21: PDB-6z22: PDB-6z23: PDB-6z24: PDB-6z25: |
Chemicals | ChemComp-GOL: ChemComp-SO4: ChemComp-CL: ChemComp-HOH: ChemComp-CEF: ChemComp-CAZ: |
Source |
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Keywords | ANTIMICROBIAL PROTEIN / beta-lactamase / antibiotic resistance / mutant / carbapenemase. / unliganded beta-lactamase / 3-layer alpha-beta-alpha sandwich / part of the DD-peptidase and beta-lactamase superfamily. |