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PDB: 5 件

1BG0
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BU of 1bg0 by Molmil
TRANSITION STATE STRUCTURE OF ARGININE KINASE
分子名称: ADENOSINE-5'-DIPHOSPHATE, ARGININE KINASE, D-ARGININE, ...
著者Zhou, G, Somasundaram, T, Blanc, E, Parthasarathy, G, Ellington, W.R, Chapman, M.S.
登録日1998-06-03
公開日1998-10-14
最終更新日2024-05-22
実験手法X-RAY DIFFRACTION (1.86 Å)
主引用文献Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions.
Proc.Natl.Acad.Sci.USA, 95, 1998
1SD0
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BU of 1sd0 by Molmil
Structure of arginine kinase C271A mutant
分子名称: ADENOSINE-5'-DIPHOSPHATE, ARGININE, Arginine kinase, ...
著者Gattis, J.L, Ruben, E, Fenley, M.O, Ellington, W.R, Chapman, M.S.
登録日2004-02-12
公開日2004-07-27
最終更新日2023-08-23
実験手法X-RAY DIFFRACTION (2.3 Å)
主引用文献The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants
Biochemistry, 43, 2004
1P50
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BU of 1p50 by Molmil
Transition state structure of an Arginine Kinase mutant
分子名称: ADENOSINE-5'-DIPHOSPHATE, ARGININE, Arginine kinase, ...
著者Pruett, P.S, Azzi, A, Clark, S.A, Yousef, M.S, Gattis, J.L, Somasundarum, T, Ellington, W.R, Chapman, M.S.
登録日2003-04-24
公開日2003-06-17
最終更新日2023-08-16
実験手法X-RAY DIFFRACTION (2.8 Å)
主引用文献The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase.
J.Biol.Chem., 278, 2003
1P52
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BU of 1p52 by Molmil
Structure of Arginine kinase E314D mutant
分子名称: ADENOSINE-5'-DIPHOSPHATE, Arginine kinase, D-ARGININE, ...
著者Pruett, P.S, Azzi, A, Clark, S.A, Yousef, M.S, Gattis, J.L, Somasundarum, T, Ellington, W.R, Chapman, M.S.
登録日2003-04-24
公開日2003-06-17
最終更新日2023-08-16
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase.
J.Biol.Chem., 278, 2003
3M10
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BU of 3m10 by Molmil
Substrate-free form of Arginine Kinase
分子名称: Arginine kinase, SULFATE ION
著者Yousef, M.S, Clark, S.A, Pruett, P.K, Somasundaram, T, Ellington, W.R, Chapman, M.S.
登録日2010-03-03
公開日2010-03-16
最終更新日2023-09-06
実験手法X-RAY DIFFRACTION (1.727 Å)
主引用文献Arginine kinase: joint crystallographic and NMR RDC analyses link substrate-associated motions to intrinsic flexibility.
J.Mol.Biol., 405, 2011

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件を2024-10-30に公開中

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