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1Y25
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BU of 1y25 by Molmil
structure of mycobacterial thiol peroxidase Tpx
分子名称: ACETATE ION, Probable thiol peroxidase
著者Stehr, M, Hoffmann, B, Jger, T, Singh, M, Hecht, H.J.
登録日2004-11-20
公開日2005-11-20
最終更新日2023-10-25
実験手法X-RAY DIFFRACTION (2.1 Å)
主引用文献Structure of the inactive variant C60S of Mycobacterium tuberculosis thiol peroxidase
Acta Crystallogr.,Sect.D, 62, 2006
1H75
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BU of 1h75 by Molmil
Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like protein NrdH-redoxin from Escherichia coli.
分子名称: GLUTAREDOXIN-LIKE PROTEIN NRDH
著者Stehr, M, Schneider, G, Aslund, F, Holmgren, A, Lindqvist, Y.
登録日2001-07-03
公開日2001-08-09
最終更新日2018-01-17
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Structural Basis for the Thioredoxin-Like Activity Profile of the Glutaredoxin-Like Nrdh-Redoxin from Escherichia Coli
J.Biol.Chem., 276, 2001
1R7H
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BU of 1r7h by Molmil
NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer
分子名称: NrdH-redoxin
著者Stehr, M, Lindqvist, Y.
登録日2003-10-21
公開日2004-05-04
最終更新日2023-08-23
実験手法X-RAY DIFFRACTION (2.69 Å)
主引用文献NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer.
Proteins, 55, 2004
2VHY
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BU of 2vhy by Molmil
Crystal structure of apo L-alanine dehydrogenase from Mycobacterium tuberculosis
分子名称: ALANINE DEHYDROGENASE
著者Agren, D, Schneider, G.
登録日2007-11-26
公開日2008-03-11
最終更新日2023-12-13
実験手法X-RAY DIFFRACTION (2.3 Å)
主引用文献Three-Dimensional Structures of Apo- and Holo-L-Alanine Dehydrogenase from Mycobacterium Tuberculosis Reveal Conformational Changes Upon Coenzyme Binding.
J.Mol.Biol., 377, 2008
2VHV
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BU of 2vhv by Molmil
Crystal structure of the D270A mutant of L-alanine dehydrogenase from Mycobacterium tuberculosis in complex with NADH.
分子名称: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ALANINE DEHYDROGENASE
著者Agren, D, Schneider, G.
登録日2007-11-26
公開日2008-03-11
最終更新日2024-05-08
実験手法X-RAY DIFFRACTION (2.8 Å)
主引用文献Three-Dimensional Structures of Apo- and Holo-L-Alanine Dehydrogenase from Mycobacterium Tuberculosis Reveal Conformational Changes Upon Coenzyme Binding.
J.Mol.Biol., 377, 2008
2VHZ
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BU of 2vhz by Molmil
Crystal structure of holo L-alanine dehydrogenase from Mycobacterium tuberculosis in the closed conformation
分子名称: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ALANINE DEHYDROGENASE
著者Agren, D, Schneider, G.
登録日2007-11-26
公開日2008-03-11
最終更新日2024-05-08
実験手法X-RAY DIFFRACTION (2.04 Å)
主引用文献Three-Dimensional Structures of Apo- and Holo-L-Alanine Dehydrogenase from Mycobacterium Tuberculosis Reveal Conformational Changes Upon Coenzyme Binding.
J.Mol.Biol., 377, 2008
2VHW
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BU of 2vhw by Molmil
Crystal structure of holo L-alanine dehydrogenase from Mycobacterium tuberculosis in the open and closed conformation
分子名称: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ALANINE DEHYDROGENASE, MAGNESIUM ION
著者Agren, D, Schneider, G.
登録日2007-11-26
公開日2008-03-11
最終更新日2024-05-08
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献Three-Dimensional Structures of Apo- and Holo-L-Alanine Dehydrogenase from Mycobacterium Tuberculosis Reveal Conformational Changes Upon Coenzyme Binding.
J.Mol.Biol., 377, 2008
2VHX
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BU of 2vhx by Molmil
Crystal structure of the ternary complex of L-alanine dehydrogenase from Mycobacterium tuberculosis with NAD+ and pyruvate
分子名称: ALANINE DEHYDROGENASE, MAGNESIUM ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ...
著者Agren, D, Schneider, G.
登録日2007-11-26
公開日2008-03-11
最終更新日2023-11-15
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献Three-Dimensional Structures of Apo- and Holo-L-Alanine Dehydrogenase from Mycobacterium Tuberculosis Reveal Conformational Changes Upon Coenzyme Binding.
J.Mol.Biol., 377, 2008
3MJO
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BU of 3mjo by Molmil
Small subunit (R2F) of native ribonucleotide reductase from Corynebacterium ammoniagenes
分子名称: MANGANESE (III) ION, Ribonucleotide reductase subunit R2F
著者Ogata, H, Stolle, P, Stehr, M, Auling, G, Lubitz, W.
登録日2010-04-13
公開日2010-08-25
最終更新日2023-09-06
実験手法X-RAY DIFFRACTION (1.36 Å)
主引用文献A Tyrosyl-Dimanganese Coupled Spin System is the Native Metalloradical Cofactor of the R2F Subunit of the Ribonucleotide Reductase of Corynebacterium ammoniagenes.
J.Am.Chem.Soc., 132, 2010

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