4ap8
From Proteopedia
(Difference between revisions)
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<StructureSection load='4ap8' size='340' side='right'caption='[[4ap8]], [[Resolution|resolution]] 2.78Å' scene=''> | <StructureSection load='4ap8' size='340' side='right'caption='[[4ap8]], [[Resolution|resolution]] 2.78Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4ap8]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4ap8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AP8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Molybdopterin_synthase Molybdopterin synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.12 2.8.1.12] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ap8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ap8 OCA], [https://pdbe.org/4ap8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ap8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ap8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ap8 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/MOC2B_HUMAN MOC2B_HUMAN]] Molybdenum cofactor deficiency type B (MOCOD type B) [MIM:[https://omim.org/entry/252150 252150]]: Autosomal recessive disease which leads to the pleiotropic loss of all molybdoenzyme activities and is characterized by severe neurological damage, neonatal seizures and early childhood death. Note=The disease is caused by mutations affecting the gene represented in this entry. |
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/MOC2B_HUMAN MOC2B_HUMAN]] Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.<ref>PMID:12732628</ref> <ref>PMID:15073332</ref> |
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:41, 25 August 2022
Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B)
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