4ap8: Difference between revisions

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<StructureSection load='4ap8' size='340' side='right'caption='[[4ap8]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
<StructureSection load='4ap8' size='340' side='right'caption='[[4ap8]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ap8]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AP8 FirstGlance]. <br>
<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'>[http://en.wikipedia.org/wiki/Molybdopterin_synthase Molybdopterin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.12 2.8.1.12] </span></td></tr>
<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ap8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ap8 OCA], [http://pdbe.org/4ap8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ap8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ap8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ap8 ProSAT]</span></td></tr>
<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 ==
[[http://www.uniprot.org/uniprot/MOC2B_HUMAN MOC2B_HUMAN]] Molybdenum cofactor deficiency type B (MOCOD type B) [MIM:[http://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.  
[[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 ==
[[http://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>   
[[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 08:41, 25 August 2022

Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B)Crystal structure of human Molybdopterin synthase catalytic subunit (MOCS2B)

Structural highlights

4ap8 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Molybdopterin synthase, with EC number 2.8.1.12
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[MOC2B_HUMAN] Molybdenum cofactor deficiency type B (MOCOD type B) [MIM: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

[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.[1] [2]

References

  1. ↑ Leimkuhler S, Freuer A, Araujo JA, Rajagopalan KV, Mendel RR. Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. J Biol Chem. 2003 Jul 11;278(28):26127-34. Epub 2003 May 5. PMID:12732628 doi:10.1074/jbc.M303092200
  2. ↑ Matthies A, Rajagopalan KV, Mendel RR, Leimkuhler S. Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5946-51. Epub 2004 Apr 8. PMID:15073332 doi:10.1073/pnas.0308191101

4ap8, resolution 2.78Å

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