Author results

3VTM
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STRUCTURE OF HEME TRANSPORT PROTEIN ISDH-NEAT3 FROM S. AUREUS IN COMPLEX WITH INDIUM-PORPHYRIN
分子名称:Iron-regulated surface determinant protein H, PROTOPORPHYRIN IX CONTAINING INDIUM, GLYCEROL
著者Vu, N.T., Caaveiro, J.M.M., Moriwaki, Y., Tsumoto, K.
登録日2012-05-31
公開日2013-05-15
最終更新日2017-11-22
実験手法X-RAY DIFFRACTION (2.8 Å)
主引用文献Selective binding of antimicrobial porphyrins to the heme-receptor IsdH-NEAT3 of Staphylococcus aureus
Protein Sci., 22, 2013
3VUA
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APO ISDH-NEAT3 IN SPACE GROUP P3121 AT A RESOLUTION OF 1.85 A
分子名称:Iron-regulated surface determinant protein H, SULFATE ION, ACETATE ION, ...
著者Vu, N.T., Caaveiro, J.M.M., Moriwaki, Y., Tsumoto, K.
登録日2012-06-26
公開日2013-06-26
最終更新日2017-11-22
実験手法X-RAY DIFFRACTION (1.85 Å)
主引用文献Structure of heme transport protein IsdH-NEAT3 from S. aureus in complex with Indium-porphyrin
To be Published
6IEJ
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THE C2 DOMAIN OF CYTOSOLIC PHOSPHOLIPASE A2 ALPHA BOUND TO PHOSPHATIDYLCHOLINE
分子名称:Cytosolic phospholipase A2, CALCIUM ION, MAGNESIUM ION, ...
著者Hirano, Y., Gao, Y.G., Stephenson, D.J., Vu, N.T., Malinina, L., Chalfant, C.E., Patel, D.J., Brown, R.E.
登録日2018-09-14
公開日2019-05-22
実験手法X-RAY DIFFRACTION (2.206 Å)
主引用文献Structural basis of phosphatidylcholine recognition by the C2-domain of cytosolic phospholipase A2alpha.
Elife, 8, 2019
3AMK
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STRUCTURE OF THE STARCH BRANCHING ENZYME I (BEI) FROM ORYZA SATIVA L
分子名称:Os06g0726400 protein, PHOSPHATE ION, GLYCEROL
著者Kakuta, Y., Chaen, K., Noguchi, J., Vu, N., Kimura, M.
登録日2010-08-20
公開日2011-09-28
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献Crystal structure of the branching enzyme I (BEI) from Oryza sativa L with implications for catalysis and substrate binding.
Glycobiology, 21, 2011
3AML
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STRUCTURE OF THE STARCH BRANCHING ENZYME I (BEI) FROM ORYZA SATIVA L
分子名称:Os06g0726400 protein, BETA-MERCAPTOETHANOL, GLYCEROL, ...
著者Kakuta, Y., Chaen, K., Noguchi, J., Vu, N., Kimura, M.
登録日2010-08-20
公開日2011-09-28
実験手法X-RAY DIFFRACTION (1.7 Å)
主引用文献Crystal structure of the branching enzyme I (BEI) from Oryza sativa L with implications for catalysis and substrate binding.
Glycobiology, 21, 2011