6gmc: Difference between revisions
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==1.2 A resolution structure of human hydroxyacid oxidase 1 bound with FMN and 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole== | |||
<StructureSection load='6gmc' size='340' side='right' caption='[[6gmc]], [[Resolution|resolution]] 1.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6gmc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GMC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C7C:5-[(4-CHLOROPHENYL)SULFANYL]-1,2,3-THIADIAZOLE-4-CARBOXYLATE'>C7C</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | |||
[[Category: | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nzl|2nzl]], [[6gmb|6gmb]]</td></tr> | ||
[[Category: | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(S)-2-hydroxy-acid_oxidase (S)-2-hydroxy-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.15 1.1.3.15] </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=6gmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gmc OCA], [http://pdbe.org/6gmc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gmc RCSB], [http://www.ebi.ac.uk/pdbsum/6gmc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gmc ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/HAOX1_HUMAN HAOX1_HUMAN]] Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate. | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arrowsmith, C H]] | |||
[[Category: Bezerra, G A]] | |||
[[Category: Bountra, C]] | |||
[[Category: Brennan, P E]] | |||
[[Category: Edwards, E]] | |||
[[Category: Krojer, T]] | [[Category: Krojer, T]] | ||
[[Category: | [[Category: MacKinnon, S]] | ||
[[Category: Oppermann, U]] | [[Category: Oppermann, U]] | ||
[[Category: | [[Category: Smee, C]] | ||
[[Category: | [[Category: Yue, W W]] | ||
[[Category: | [[Category: Fmn]] | ||
[[Category: Glycolate]] | |||
[[Category: Glyoxylate]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Peroxisome]] | |||
[[Category: Primary hyperoxaluria]] | |||
Revision as of 07:46, 14 June 2018
1.2 A resolution structure of human hydroxyacid oxidase 1 bound with FMN and 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole
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