3d4s

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Cholesterol bound form of human beta2 adrenergic receptor.==
==Cholesterol bound form of human beta2 adrenergic receptor.==
-
<StructureSection load='3d4s' size='340' side='right' caption='[[3d4s]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+
<StructureSection load='3d4s' size='340' side='right'caption='[[3d4s]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3d4s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D4S FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3d4s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D4S FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=TIM:(2S)-1-(TERT-BUTYLAMINO)-3-[(4-MORPHOLIN-4-YL-1,2,5-THIADIAZOL-3-YL)OXY]PROPAN-2-OL'>TIM</scene></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=TIM:(2S)-1-(TERT-BUTYLAMINO)-3-[(4-MORPHOLIN-4-YL-1,2,5-THIADIAZOL-3-YL)OXY]PROPAN-2-OL'>TIM</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rh1|2rh1]]</td></tr>
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rh1|2rh1]]</div></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADRB2, ADRB2R, B2AR / E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADRB2, ADRB2R, B2AR / E ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3d4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d4s OCA], [http://pdbe.org/3d4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3d4s RCSB], [http://www.ebi.ac.uk/pdbsum/3d4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3d4s ProSAT]</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=3d4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d4s OCA], [https://pdbe.org/3d4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d4s RCSB], [https://www.ebi.ac.uk/pdbsum/3d4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d4s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/ADRB2_HUMAN ADRB2_HUMAN]] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
+
[[https://www.uniprot.org/uniprot/ADRB2_HUMAN ADRB2_HUMAN]] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 30: Line 30:
</div>
</div>
<div class="pdbe-citations 3d4s" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3d4s" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
 +
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 35: Line 39:
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
 +
[[Category: Large Structures]]
[[Category: ATCG3D, Accelerated Technologies Center for Gene to 3D Structure]]
[[Category: ATCG3D, Accelerated Technologies Center for Gene to 3D Structure]]
[[Category: Cherezov, V]]
[[Category: Cherezov, V]]

Revision as of 19:19, 20 October 2021

Cholesterol bound form of human beta2 adrenergic receptor.

PDB ID 3d4s

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools