6mxt

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Current revision (06:41, 11 October 2023) (edit) (undo)
 
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<StructureSection load='6mxt' size='340' side='right'caption='[[6mxt]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
<StructureSection load='6mxt' size='340' side='right'caption='[[6mxt]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6mxt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama] and [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6csy 6csy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MXT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MXT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6mxt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6csy 6csy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MXT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=K5Y:salmeterol'>K5Y</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9593422&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=K5Y:salmeterol'>K5Y</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADRB2, ADRB2R, B2AR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mxt OCA], [https://pdbe.org/6mxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mxt RCSB], [https://www.ebi.ac.uk/pdbsum/6mxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mxt ProSAT]</span></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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<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=6mxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mxt OCA], [http://pdbe.org/6mxt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mxt RCSB], [http://www.ebi.ac.uk/pdbsum/6mxt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mxt ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[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.[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
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*[[Antibody 3D structures|Antibody 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Camelus glama]]
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[[Category: Escherichia virus T4]]
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Lama glama]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lysozyme]]
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[[Category: Bouvier M]]
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[[Category: Bouvier, M]]
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[[Category: Dror RO]]
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[[Category: Dror, R O]]
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[[Category: Kobilka BK]]
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[[Category: Kobilka, B K]]
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[[Category: Mahoney JP]]
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[[Category: Mahoney, J P]]
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[[Category: Masureel M]]
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[[Category: Masureel, M]]
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[[Category: Mildorf TJ]]
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[[Category: Mildorf, T J]]
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[[Category: Pardon E]]
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[[Category: Pardon, E]]
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[[Category: Picard LP]]
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[[Category: Picard, L P]]
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[[Category: Rodrigues JPGLM]]
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[[Category: Rodrigues, J P.G L.M]]
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[[Category: Shaw DE]]
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[[Category: Shaw, D E]]
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[[Category: Steyaert J]]
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[[Category: Steyaert, J]]
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[[Category: Sunahara RK]]
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[[Category: Sunahara, R K]]
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[[Category: Weis WI]]
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[[Category: Weis, W I]]
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[[Category: Zhang C]]
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[[Category: Westhuizen, E van der]]
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[[Category: Zou Y]]
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[[Category: Zhang, C]]
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[[Category: Van der Westhuizen E]]
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[[Category: Zou, Y]]
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[[Category: Active conformation]]
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[[Category: Adrenergic receptor]]
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[[Category: Asthma drug]]
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[[Category: G protein-coupled receptor]]
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[[Category: Membrane protein]]
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[[Category: Nanobody]]
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[[Category: Signaling protein-hormone complex]]
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Current revision

Crystal structure of human beta2 adrenergic receptor bound to salmeterol and Nb71

PDB ID 6mxt

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