3a2j
From Proteopedia
(Difference between revisions)
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| + | [[Image:3a2j.jpg|left|200px]] | ||
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| + | {{STRUCTURE_3a2j| PDB=3a2j | SCENE= }} | ||
| - | + | ===Crystal structure of the human vitamin D receptor (H305F/H397F) ligand binding domain complexed with TEI-9647=== | |
| - | Description: Crystal structure of the human vitamin D receptor (H305F/H397F) ligand binding domain complexed with TEI-9647 | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ==About this Structure== |
| + | 3A2J is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A2J OCA]. | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Kakuda, S.]] | ||
| + | [[Category: Takimoto-Kamimura, M.]] | ||
| + | [[Category: Activator]] | ||
| + | [[Category: Alternative splicing]] | ||
| + | [[Category: Disease mutation]] | ||
| + | [[Category: Dna-binding]] | ||
| + | [[Category: Hormone receptor]] | ||
| + | [[Category: Hormone/growth factor receptor]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Nucleus]] | ||
| + | [[Category: Phosphoprotein]] | ||
| + | [[Category: Polymorphism]] | ||
| + | [[Category: Receptor]] | ||
| + | [[Category: Transcription]] | ||
| + | [[Category: Transcription regulation]] | ||
| + | [[Category: Zinc]] | ||
| + | [[Category: Zinc-finger]] | ||
| + | |||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 26 08:29:40 2010'' | ||
Revision as of 04:25, 26 May 2010
Crystal structure of the human vitamin D receptor (H305F/H397F) ligand binding domain complexed with TEI-9647
About this Structure
3A2J is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Page seeded by OCA on Wed May 26 08:29:40 2010
Categories: Homo sapiens | Kakuda, S. | Takimoto-Kamimura, M. | Activator | Alternative splicing | Disease mutation | Dna-binding | Hormone receptor | Hormone/growth factor receptor | Metal-binding | Nucleus | Phosphoprotein | Polymorphism | Receptor | Transcription | Transcription regulation | Zinc | Zinc-finger
