3vz6: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Crystal Structure Analysis of the Mini-chaperonines, variant with Gly 184 replaced with Ile and Leu 185 replaced Val and Val 186 replaced with Leu.==
-<StructureSection load='3vz6' size='340' side='right' caption='[[3vz6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+<StructureSection load='3vz6' size='340' side='right'caption='[[3vz6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3vz6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VZ6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3vz6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VZ6 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vz7|3vz7]], [[3vz8|3vz8]]</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]] 1.5&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">groL, groEL, mopA, b4143, JW4103 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3vz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vz6 OCA], [https://pdbe.org/3vz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vz6 RCSB], [https://www.ebi.ac.uk/pdbsum/3vz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vz6 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vz6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vz6 RCSB], [http://www.ebi.ac.uk/pdbsum/3vz6 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600]  Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
+[https://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600]  Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
 ==See Also==
-*[[Chaperonin|Chaperonin]]
+*[[Chaperonin 3D structures|Chaperonin 3D structures]]
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
-[[Category: Saijo, S]]
+[[Category: Large Structures]]
-[[Category: Sato, T]]
+[[Category: Saijo S]]
-[[Category: Atp-binding]]
+[[Category: Sato T]]
-[[Category: Cell division]]
-[[Category: Chaperone]]
-[[Category: Chaperonin]]
-[[Category: Groel]]
-[[Category: Hsp60]]
-[[Category: Phosphorylation]]