5mpo: Difference between revisions

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<StructureSection load='5mpo' size='340' side='right'caption='[[5mpo]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
<StructureSection load='5mpo' size='340' side='right'caption='[[5mpo]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5mpo]] 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=5MPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MPO FirstGlance]. <br>
<table><tr><td colspan='2'>[[5mpo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MPO FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MOCS2, MOCO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MOCS2, MCBPE, MOCO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.43&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mpo OCA], [https://pdbe.org/5mpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mpo RCSB], [https://www.ebi.ac.uk/pdbsum/5mpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mpo ProSAT]</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=5mpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mpo OCA], [http://pdbe.org/5mpo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mpo RCSB], [http://www.ebi.ac.uk/pdbsum/5mpo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mpo ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/MOC2A_HUMAN MOC2A_HUMAN]] Sulfite oxidase deficiency due to molybdenum cofactor deficiency type B. The disease is caused by mutations affecting the gene represented in this entry. [[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/MOC2A_HUMAN MOC2A_HUMAN] Sulfite oxidase deficiency due to molybdenum cofactor deficiency type B. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MOC2A_HUMAN MOC2A_HUMAN]] Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin.[HAMAP-Rule:MF_03051]<ref>PMID:12732628</ref> [[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/MOC2A_HUMAN MOC2A_HUMAN] Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin.[HAMAP-Rule:MF_03051]<ref>PMID:12732628</ref>  
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Molybdopterin synthase]]
[[Category: Arrowsmith C]]
[[Category: Arrowsmith, C]]
[[Category: Bailey H]]
[[Category: Bailey, H]]
[[Category: Bountra C]]
[[Category: Bountra, C]]
[[Category: Burgess-Brown N]]
[[Category: Burgess-Brown, N]]
[[Category: Edwards A]]
[[Category: Delft, F von]]
[[Category: Fitzpatrick F]]
[[Category: Edwards, A]]
[[Category: Kopec J]]
[[Category: Fitzpatrick, F]]
[[Category: Oberholzer AE]]
[[Category: Kopec, J]]
[[Category: Strain-Damerell C]]
[[Category: Oberholzer, A E]]
[[Category: Williams E]]
[[Category: Strain-Damerell, C]]
[[Category: Yue WW]]
[[Category: Williams, E]]
[[Category: Von Delft F]]
[[Category: Yue, W W]]
[[Category: Mocs2a]]
[[Category: Mocs2b]]
[[Category: Transferase]]

Latest revision as of 17:43, 8 November 2023

Crystal structure of human molybdopterin synthase complex

5mpo, resolution 2.43Å

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