5d5a

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'''Unreleased structure'''
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==In meso in situ serial X-ray crystallography structure of the Beta2-adrenergic receptor at 100 K==
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<StructureSection load='5d5a' size='340' side='right' caption='[[5d5a]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
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The entry 5d5a is ON HOLD until Paper Publication
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5d5a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D5A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D5A FirstGlance]. <br>
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Authors: Huang, C.-Y.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=ACM:ACETAMIDE'>ACM</scene>, <scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=CAU:(2S)-1-(9H-CARBAZOL-4-YLOXY)-3-(ISOPROPYLAMINO)PROPAN-2-OL'>CAU</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=N9S:4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSE'>N9S</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
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Description:
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<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=5d5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d5a OCA], [http://pdbe.org/5d5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d5a RCSB], [http://www.ebi.ac.uk/pdbsum/5d5a PDBsum]</span></td></tr>
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[[Category: Unreleased Structures]]
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</table>
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[[Category: Huang, C.-Y]]
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== Function ==
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[[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.
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__TOC__
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</StructureSection>
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[[Category: Lysozyme]]
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[[Category: Caffrey, M]]
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[[Category: Diederichs, K Kay]]
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[[Category: Huang, C Y]]
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[[Category: Kobilka, B]]
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[[Category: Liu, X]]
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[[Category: Olieric, V]]
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[[Category: Wang, M]]
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[[Category: Warshamanage, R]]
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[[Category: Hydrolase]]
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[[Category: Membrane protein]]
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[[Category: Membrane protein-hydrolase complex]]

Revision as of 20:30, 13 January 2016

In meso in situ serial X-ray crystallography structure of the Beta2-adrenergic receptor at 100 K

5d5a, resolution 2.48Å

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