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1OLU
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BU of 1olu by Molmil
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase
Descriptor: 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT, 2-OXOISOVALERATE DEHYDROGENASE BETA SUBUNIT, GLYCEROL, ...
Authors:Wynn, R.M, Machius, M, Chuang, J.L, Li, J, Tomchick, D.R, Chuang, D.T.
Deposit date:2003-08-15
Release date:2003-08-28
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Roles of His291-Alpha and His146-Beta' in the Reductive Acylation Reaction Catalyzed by Human Branched-Chain Alpha-Ketoacid Dehydrogenase: Refined Phosphorylation Loop Structure in the Active Site.
J.Biol.Chem., 278, 2003
1OLS
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BU of 1ols by Molmil
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase
Descriptor: 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT, 2-OXOISOVALERATE DEHYDROGENASE BETA SUBUNIT, GLYCEROL, ...
Authors:Wynn, R.M, Machius, M, Chuang, J.L, Li, J, Tomchick, D.R, Chuang, D.T.
Deposit date:2003-08-12
Release date:2003-08-15
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Roles of His291-Alpha and His146-Beta' in the Reductive Acylation Reaction Catalyzed by Human Branched-Chain Alpha-Ketoacid Dehydrogenase: Refined Phosphorylation Loop Structure in the Active Site.
J.Biol.Chem., 278, 2003
1OLX
DownloadVisualize
BU of 1olx by Molmil
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase
Descriptor: 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT, 2-OXOISOVALERATE DEHYDROGENASE BETA SUBUNIT, GLYCEROL, ...
Authors:Wynn, R.M, Machius, M, Chuang, J.L, Li, J, Tomchick, D.R, Chuang, D.T.
Deposit date:2003-08-18
Release date:2003-08-28
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.25 Å)
Cite:Roles of His291-Alpha and His146-Beta' in the Reductive Acylation Reaction Catalyzed by Human Branched-Chain Alpha-Ketoacid Dehydrogenase: Refined Phosphorylation Loop Structure in the Active Site.
J.Biol.Chem., 278, 2003
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