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.


1bc5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:59, 2 August 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='1bc5' size='340' side='right'caption='[[1bc5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1bc5' size='340' side='right'caption='[[1bc5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1bc5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BC5 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1bc5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BC5 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 2.2&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-glutamate_O-methyltransferase Protein-glutamate O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.80 2.1.1.80] </span></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=1bc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bc5 OCA], [https://pdbe.org/1bc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bc5 RCSB], [https://www.ebi.ac.uk/pdbsum/1bc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bc5 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=1bc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bc5 OCA], [http://pdbe.org/1bc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bc5 RCSB], [http://www.ebi.ac.uk/pdbsum/1bc5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bc5 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/CHER_SALTY CHER_SALTY]] Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
+
[https://www.uniprot.org/uniprot/CHER_SALTY CHER_SALTY] Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 33: Line 32:
==See Also==
==See Also==
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
-
*[[Molecular Playground/CheR|Molecular Playground/CheR]]
 
*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]]
*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]]
== References ==
== References ==
Line 40: Line 38:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Protein-glutamate O-methyltransferase]]
+
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-
[[Category: Djordjevic, S]]
+
[[Category: Djordjevic S]]
-
[[Category: Stock, A M]]
+
[[Category: Stock AM]]
-
[[Category: Chemotaxis receptor]]
+
-
[[Category: Methyltransferase]]
+
-
[[Category: Peptide binding]]
+

Current revision

CHEMOTAXIS RECEPTOR RECOGNITION BY PROTEIN METHYLTRANSFERASE CHER

PDB ID 1bc5

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/1bc5"
Personal tools