4K9S
| Peptidoglycan O-acetylesterase in action, setmet | 分子名称: | GDSL-like Lipase/Acylhydrolase family protein | 著者 | Williams, A.H, Gompert Boneca, I. | 登録日 | 2013-04-21 | 公開日 | 2014-09-03 | 最終更新日 | 2014-10-22 | 実験手法 | X-RAY DIFFRACTION (2.334 Å) | 主引用文献 | Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members. Acta Crystallogr.,Sect.D, 70, 2014
|
|
4K40
| Peptidoglycan O-acetylesterase in action, 0 min | 分子名称: | GDSL-like Lipase/Acylhydrolase family protein | 著者 | Williams, A.H, Gompert Boneca, I. | 登録日 | 2013-04-11 | 公開日 | 2014-09-03 | 最終更新日 | 2017-06-21 | 実験手法 | X-RAY DIFFRACTION (2.634 Å) | 主引用文献 | Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members. Acta Crystallogr.,Sect.D, 70, 2014
|
|
4K7J
| Peptidoglycan O-acetylesterase in action, 5 min | 分子名称: | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ACETATE ION, GDSL-like Lipase/Acylhydrolase family protein | 著者 | Williams, A.H, Gomperts Boneca, I. | 登録日 | 2013-04-17 | 公開日 | 2014-09-03 | 最終更新日 | 2014-10-22 | 実験手法 | X-RAY DIFFRACTION (1.968 Å) | 主引用文献 | Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members. Acta Crystallogr.,Sect.D, 70, 2014
|
|
4K3U
| Peptidoglycan O-acetylesterase in action, 30 min | 分子名称: | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, GDSL-like Lipase/Acylhydrolase family protein | 著者 | Williams, A.H, Gomperts Boneca, I. | 登録日 | 2013-04-11 | 公開日 | 2014-09-03 | 最終更新日 | 2014-10-22 | 実験手法 | X-RAY DIFFRACTION (2.158 Å) | 主引用文献 | Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members. Acta Crystallogr.,Sect.D, 70, 2014
|
|