6JV0
 
 | | Crystal Structure of N-terminal domain of ArgZ, bound to Product, an arginine dihydrolase from the Ornithine-Ammonia Cycle in Cyanobacteria | | Descriptor: | 1,2-ETHANEDIOL, L-ornithine, Sll1336 protein | | Authors: | Zhuang, N, Li, L, Wu, X, Zhang, Y. | | Deposit date: | 2019-04-15 | | Release date: | 2020-01-15 | | Last modified: | 2024-03-27 | | Method: | X-RAY DIFFRACTION (1.14 Å) | | Cite: | Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond rotation" catalytic mechanism.
J.Biol.Chem., 295, 2020
|
|
6JV1
 | | Crystal Structure of N-terminal domain of ArgZ, C264S mutant, bound to Substrate, an arginine dihydrolase from the Ornithine-Ammonia Cycle in Cyanobacteria | | Descriptor: | ARGININE, Sll1336 protein | | Authors: | Zhuang, N, Li, L, Wu, X, Zhang, Y. | | Deposit date: | 2019-04-15 | | Release date: | 2020-01-15 | | Last modified: | 2023-11-22 | | Method: | X-RAY DIFFRACTION (1.2 Å) | | Cite: | Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond rotation" catalytic mechanism.
J.Biol.Chem., 295, 2020
|
|
6JUY
 | | Crystal Structure of ArgZ, apo structure, an Arginine Dihydrolase from the Ornithine-Ammonia Cycle in Cyanobacteria | | Descriptor: | Sll1336 protein | | Authors: | Zhuang, N, Li, L, Wu, X, Zhang, Y. | | Deposit date: | 2019-04-15 | | Release date: | 2020-01-15 | | Last modified: | 2023-11-22 | | Method: | X-RAY DIFFRACTION (2.97 Å) | | Cite: | Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond rotation" catalytic mechanism.
J.Biol.Chem., 295, 2020
|
|
6JUZ
 | | Crystal Structure of N-terminal domain of ArgZ(N71S) covalently bond to a reaction intermediate | | Descriptor: | 1,2-ETHANEDIOL, ARGININE, Sll1336 protein | | Authors: | Zhuang, N, Li, L, Wu, X, Zhuang, Y. | | Deposit date: | 2019-04-15 | | Release date: | 2020-01-15 | | Last modified: | 2023-11-22 | | Method: | X-RAY DIFFRACTION (1.21 Å) | | Cite: | Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond rotation" catalytic mechanism.
J.Biol.Chem., 295, 2020
|
|
