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5fq2

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Current revision (13:18, 26 July 2023) (edit) (undo)
 
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<StructureSection load='5fq2' size='340' side='right'caption='[[5fq2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5fq2' size='340' side='right'caption='[[5fq2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fq2]] is a 2 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=5FQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FQ2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5fq2]] is a 2 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=5FQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FQ2 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LDH:N~6~-ETHYL-L-LYSINE'>LDH</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.201&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fq2 OCA], [http://pdbe.org/5fq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fq2 RCSB], [http://www.ebi.ac.uk/pdbsum/5fq2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fq2 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDH:N~6~-ETHYL-L-LYSINE'>LDH</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fq2 OCA], [https://pdbe.org/5fq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fq2 RCSB], [https://www.ebi.ac.uk/pdbsum/5fq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fq2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/UBC9_HUMAN UBC9_HUMAN]] Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation.<ref>PMID:8668529</ref> <ref>PMID:11451954</ref> <ref>PMID:15809060</ref> <ref>PMID:19744555</ref> <ref>PMID:19638400</ref> <ref>PMID:17466333</ref> <ref>PMID:20077568</ref> [[http://www.uniprot.org/uniprot/SAE2_HUMAN SAE2_HUMAN]] The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.<ref>PMID:11481243</ref> <ref>PMID:11451954</ref> <ref>PMID:19443651</ref> <ref>PMID:15660128</ref> <ref>PMID:17643372</ref> <ref>PMID:20164921</ref>
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[https://www.uniprot.org/uniprot/UBC9_HUMAN UBC9_HUMAN] Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation.<ref>PMID:8668529</ref> <ref>PMID:11451954</ref> <ref>PMID:15809060</ref> <ref>PMID:19744555</ref> <ref>PMID:19638400</ref> <ref>PMID:17466333</ref> <ref>PMID:20077568</ref>
==See Also==
==See Also==
*[[SUMO conjugating enzyme Ubc9|SUMO conjugating enzyme Ubc9]]
*[[SUMO conjugating enzyme Ubc9|SUMO conjugating enzyme Ubc9]]
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*[[Ubiquitin activating enzyme|Ubiquitin activating enzyme]]
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*[[3D structures of Ubiquitin activating enzyme|3D structures of Ubiquitin activating enzyme]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Castano, L]]
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[[Category: Castano L]]
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[[Category: Liu, B]]
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[[Category: Liu B]]
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[[Category: Lois, M]]
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[[Category: Lois M]]
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[[Category: Reverter, D]]
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[[Category: Reverter D]]
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[[Category: Activating enzyme]]
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[[Category: Conjugating enzyme]]
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[[Category: Ligase]]
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[[Category: Sumo]]
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Current revision

Crystal structure of human SUMO E1 UFD domain in complex with Ubc9 in a P422 space group.

PDB ID 5fq2

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