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1iy0
From Proteopedia
(Difference between revisions)
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<StructureSection load='1iy0' size='340' side='right'caption='[[1iy0]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='1iy0' size='340' side='right'caption='[[1iy0]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1iy0]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1iy0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IY0 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]] 2.95Å</td></tr> |
| - | <tr id=' | + | <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></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=1iy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iy0 OCA], [https://pdbe.org/1iy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iy0 RCSB], [https://www.ebi.ac.uk/pdbsum/1iy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iy0 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/FTSH_THET8 FTSH_THET8] Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (By similarity).[HAMAP-Rule:MF_01458] Degrades preferentially unfolded substrates in a processive, ATP-dependent manner, usually after hydrophobic residues.[HAMAP-Rule:MF_01458] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Makyio | + | [[Category: Thermus thermophilus]] |
| - | [[Category: Morikawa | + | [[Category: Makyio H]] |
| - | [[Category: Niwa | + | [[Category: Morikawa K]] |
| - | [[Category: Tsuchiya | + | [[Category: Niwa H]] |
| - | [[Category: Yoshida | + | [[Category: Tsuchiya D]] |
| - | + | [[Category: Yoshida M]] | |
| - | + | ||
Current revision
Crystal structure of the FtsH ATPase domain with AMP-PNP from Thermus thermophilus
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