This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1iy1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (23:38, 27 December 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='1iy1' size='340' side='right'caption='[[1iy1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1iy1' size='340' side='right'caption='[[1iy1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1iy1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IY1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1IY1 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1iy1]] 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=1IY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IY1 FirstGlance]. <br>
-
</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></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ixz|1ixz]], [[1iy0|1iy0]], [[1iy2|1iy2]]</div></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></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FtsH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</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=1iy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iy1 OCA], [https://pdbe.org/1iy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iy1 RCSB], [https://www.ebi.ac.uk/pdbsum/1iy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iy1 ProSAT]</span></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1iy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iy1 OCA], [http://pdbe.org/1iy1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iy1 RCSB], [http://www.ebi.ac.uk/pdbsum/1iy1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iy1 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://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]
+
[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]]
Line 34: Line 33:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Makyio, H]]
+
[[Category: Thermus thermophilus]]
-
[[Category: Morikawa, K]]
+
[[Category: Makyio H]]
-
[[Category: Niwa, H]]
+
[[Category: Morikawa K]]
-
[[Category: Tsuchiya, D]]
+
[[Category: Niwa H]]
-
[[Category: Yoshida, M]]
+
[[Category: Tsuchiya D]]
-
[[Category: Aaa domain fold]]
+
[[Category: Yoshida M]]
-
[[Category: Hydrolase]]
+

Current revision

Crystal structure of the FtsH ATPase domain with ADP from Thermus thermophilus

PDB ID 1iy1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iy1"
Personal tools