5mpo
From Proteopedia
(Difference between revisions)
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<StructureSection load='5mpo' size='340' side='right'caption='[[5mpo]], [[Resolution|resolution]] 2.43Å' scene=''> | <StructureSection load='5mpo' size='340' side='right'caption='[[5mpo]], [[Resolution|resolution]] 2.43Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5mpo]] is a 4 chain structure with sequence from [ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.43Å</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'>[ | + | |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [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 == | ||
| - | [ | + | [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: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Arrowsmith C]] | |
| - | [[Category: Arrowsmith | + | [[Category: Bailey H]] |
| - | [[Category: Bailey | + | [[Category: Bountra C]] |
| - | [[Category: Bountra | + | [[Category: Burgess-Brown N]] |
| - | [[Category: Burgess-Brown | + | [[Category: Edwards A]] |
| - | + | [[Category: Fitzpatrick F]] | |
| - | [[Category: Edwards | + | [[Category: Kopec J]] |
| - | [[Category: Fitzpatrick | + | [[Category: Oberholzer AE]] |
| - | [[Category: Kopec | + | [[Category: Strain-Damerell C]] |
| - | [[Category: Oberholzer | + | [[Category: Williams E]] |
| - | [[Category: Strain-Damerell | + | [[Category: Yue WW]] |
| - | [[Category: Williams | + | [[Category: Von Delft F]] |
| - | [[Category: Yue | + | |
| - | [[Category: | + | |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of human molybdopterin synthase complex
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