5ac2: Difference between revisions
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''' | ==human aldehyde dehydrogenase 1A1 with duocarmycin analog== | ||
<StructureSection load='5ac2' size='340' side='right' caption='[[5ac2]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ac2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AC2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AC2 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K9P:1-[(1S)-1-METHYL-5-OXIDANYL-1,2-DIHYDROBENZO[E]INDOL-3-YL]HEXAN-1-ONE'>K9P</scene>, <scene name='pdbligand=TXE:[[(2R,3S,4R,5R)-5-[(3R)-3-AMINOCARBONYL-3,4-DIHYDRO-2H-PYRIDIN-1-YL]-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANIDYL-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHYL+PHOSPHATE'>TXE</scene>, <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5abm|5abm]], [[5ac0|5ac0]], [[5ac1|5ac1]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Retinal_dehydrogenase Retinal dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.36 1.2.1.36] </span></td></tr> | |||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ac2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ac2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ac2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ac2 PDBsum]</span></td></tr> | ||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/AL1A1_HUMAN AL1A1_HUMAN]] Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity). | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Retinal dehydrogenase]] | |||
[[Category: Blank, I D]] | |||
[[Category: Harteis, S]] | |||
[[Category: Koch, M F]] | |||
[[Category: Ochsenfeld, C]] | |||
[[Category: Pestel, G]] | [[Category: Pestel, G]] | ||
[[Category: Schneider, S]] | [[Category: Schneider, S]] | ||
[[Category: | [[Category: Sieber, S A]] | ||
[[Category: | [[Category: Tietze, L F]] | ||
[[Category: | [[Category: Aldehyde dehydrogenase activity]] | ||
[[Category: | [[Category: Oxidation-reduction process]] | ||
[[Category: Oxidoreductase]] | |||
Revision as of 13:37, 26 August 2015
human aldehyde dehydrogenase 1A1 with duocarmycin analog
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