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3fht
From Proteopedia
(Difference between revisions)
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==Crystal structure of human Dbp5 in complex with AMPPNP and RNA== | ==Crystal structure of human Dbp5 in complex with AMPPNP and RNA== | ||
| - | <StructureSection load='3fht' size='340' side='right' caption='[[3fht]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='3fht' size='340' side='right'caption='[[3fht]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3fht]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3fht]] 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=3FHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FHT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fhc|3fhc]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fhc|3fhc]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX19B (Dbp5) ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX19B (Dbp5) ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3fht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fht OCA], [https://pdbe.org/3fht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fht RCSB], [https://www.ebi.ac.uk/pdbsum/3fht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fht ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/DD19B_HUMAN DD19B_HUMAN]] ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 32: | Line 32: | ||
==See Also== | ==See Also== | ||
| - | *[[Helicase|Helicase]] | + | *[[Helicase 3D structures|Helicase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Conti, E]] | [[Category: Conti, E]] | ||
[[Category: Moeller, H von]] | [[Category: Moeller, H von]] | ||
Revision as of 08:01, 2 March 2022
Crystal structure of human Dbp5 in complex with AMPPNP and RNA
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Categories: Human | Large Structures | Conti, E | Moeller, H von | Atp-binding | Can | Dbp5 | Ddx19b | Dead-box helicase | Gle1 | Helicase | Hydrolase | Hydrolase-rna complex | Membrane | Mrna export | Mrna transport | Nuclear pore | Nuclear pore complex | Nucleocytoplasmic transport | Nucleotide-binding | Nucleus | Nup159 | Nup214 | Phosphoprotein | Protein transport | Rna dependent atpase | Rna-binding | Translocation | Transport

