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-Structure paper
Title | Recognition of the beta-lactam carboxylate triggers acylation ofNeisseria gonorrhoeaepenicillin-binding protein 2. |
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Journal, issue, pages | J. Biol. Chem., Vol. 294, Page 14020-14032, Year 2019 |
Publish date | May 29, 2019 (structure data deposition date) |
![]() | Singh, A. / Tomberg, J. / Nicholas, R.A. / Davies, C. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.74 - 1.92 Å |
Structure data | ![]() PDB-6p52: ![]() PDB-6p53: ![]() PDB-6p54: ![]() PDB-6p55: ![]() PDB-6p56: |
Chemicals | ![]() ChemComp-PO4: ![]() ChemComp-HOH: ![]() ChemComp-NZV: ![]() ChemComp-CEF: ![]() ChemComp-9F2: ![]() ChemComp-PEG: ![]() ChemComp-NZM: |
Source |
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![]() | HYDROLASE / Penicillin-binding protein / transpeptidase domain / N. gonorrhoease antibiotic resistance / N. gonorrhoeae / antibiotic resistance / HYDROLASE/ANTIBIOTIC / Neisseria gonorrhoeae / HYDROLASE-ANTIBIOTIC complex |