3vkg
From Proteopedia
(Difference between revisions)
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:3vkg.png|left|200px]] | ||
| - | + | ==X-ray structure of an MTBD truncation mutant of dynein motor domain== | |
| - | + | <StructureSection load='3vkg' size='340' side='right'caption='[[3vkg]], [[Resolution|resolution]] 2.81Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3vkg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VKG FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.81Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</scene></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=3vkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vkg OCA], [https://pdbe.org/3vkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vkg RCSB], [https://www.ebi.ac.uk/pdbsum/3vkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vkg ProSAT]</span></td></tr> |
| - | [[3vkg]] is a 2 chain structure | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DYHC_DICDI DYHC_DICDI] Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. | ||
==See Also== | ==See Also== | ||
| - | *[[Dynein|Dynein]] | + | *[[Dynein 3D structures|Dynein 3D structures]] |
| - | [[Category: Dictyostelium discoideum | + | __TOC__ |
| - | [[Category: Kon | + | </StructureSection> |
| - | [[Category: Kurisu | + | [[Category: Dictyostelium discoideum]] |
| - | [[Category: Oyama | + | [[Category: Large Structures]] |
| - | [[Category: Shimo-Kon | + | [[Category: Kon T]] |
| - | [[Category: Suto | + | [[Category: Kurisu G]] |
| - | + | [[Category: Oyama T]] | |
| - | + | [[Category: Shimo-Kon R]] | |
| - | + | [[Category: Suto K]] | |
| - | + | ||
Current revision
X-ray structure of an MTBD truncation mutant of dynein motor domain
| |||||||||||
