1htl
From Proteopedia
(Difference between revisions)
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<StructureSection load='1htl' size='340' side='right'caption='[[1htl]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1htl' size='340' side='right'caption='[[1htl]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1htl]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1htl]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTL FirstGlance]. <br> |
| - | </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=1htl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htl OCA], [https://pdbe.org/1htl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htl RCSB], [https://www.ebi.ac.uk/pdbsum/1htl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htl ProSAT]</span></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]] 2.5Å</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=1htl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htl OCA], [https://pdbe.org/1htl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htl RCSB], [https://www.ebi.ac.uk/pdbsum/1htl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ELBP_ECOLX ELBP_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. | |
== 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: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hol | + | [[Category: Hol WGJ]] |
| - | [[Category: Merritt | + | [[Category: Merritt EA]] |
| - | + | ||
Revision as of 11:35, 27 March 2024
MUTATION OF A BURIED RESIDUE CAUSES LACK OF ACTIVITY BUT NO CONFORMATIONAL CHANGE: CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN MUTANT VAL 97--> LYS
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