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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) |
![]() | Tooke, C.L. / Hinchliffe, P. / Bonomo, R.A. / Schofield, C.J. / Mulholland, A.J. / Spencer, J. |
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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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![]() | 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. |