5x1b

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==CO bound cytochrome c oxidase at 20 nsec after pump laser irradiation to release CO from O2 reduction center==
==CO bound cytochrome c oxidase at 20 nsec after pump laser irradiation to release CO from O2 reduction center==
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<StructureSection load='5x1b' size='340' side='right' caption='[[5x1b]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='5x1b' size='340' side='right'caption='[[5x1b]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5x1b]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X1B FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5x1b]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X1B 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=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEK:(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(STEAROYLOXY)METHYL]ETHYL+(5E,8E,11E,14E)-ICOSA-5,8,11,14-TETRAENOATE'>PEK</scene>, <scene name='pdbligand=PGV:(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+(11E)-OCTADEC-11-ENOATE'>PGV</scene>, <scene name='pdbligand=PSC:(7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-17,20-DIEN-1-AMINIUM+4-OXIDE'>PSC</scene>, <scene name='pdbligand=TGL:TRISTEAROYLGLYCEROL'>TGL</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.4&#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=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEK:(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(STEAROYLOXY)METHYL]ETHYL+(5E,8E,11E,14E)-ICOSA-5,8,11,14-TETRAENOATE'>PEK</scene>, <scene name='pdbligand=PGV:(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+(11E)-OCTADEC-11-ENOATE'>PGV</scene>, <scene name='pdbligand=PSC:(7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-17,20-DIEN-1-AMINIUM+4-OXIDE'>PSC</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene>, <scene name='pdbligand=TGL:TRISTEAROYLGLYCEROL'>TGL</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x19|5x19]], [[5x1f|5x1f]]</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=5x1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x1b OCA], [https://pdbe.org/5x1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x1b RCSB], [https://www.ebi.ac.uk/pdbsum/5x1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x1b 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/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] </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=5x1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x1b OCA], [http://pdbe.org/5x1b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x1b RCSB], [http://www.ebi.ac.uk/pdbsum/5x1b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x1b ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/COX5B_BOVIN COX5B_BOVIN]] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [[http://www.uniprot.org/uniprot/COX7B_BOVIN COX7B_BOVIN]] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [[http://www.uniprot.org/uniprot/COX3_BOVIN COX3_BOVIN]] Subunits I, II and III form the functional core of the enzyme complex. [[http://www.uniprot.org/uniprot/CX6A2_BOVIN CX6A2_BOVIN]] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [[http://www.uniprot.org/uniprot/COX6C_BOVIN COX6C_BOVIN]] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [[http://www.uniprot.org/uniprot/COX7C_BOVIN COX7C_BOVIN]] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [[http://www.uniprot.org/uniprot/COX2_BOVIN COX2_BOVIN]] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1. [[http://www.uniprot.org/uniprot/CX6B1_BOVIN CX6B1_BOVIN]] Connects the two COX monomers into the physiological dimeric form. [[http://www.uniprot.org/uniprot/COX1_BOVIN COX1_BOVIN]] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. [[http://www.uniprot.org/uniprot/COX41_BOVIN COX41_BOVIN]] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [[http://www.uniprot.org/uniprot/COX8B_BOVIN COX8B_BOVIN]] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [[http://www.uniprot.org/uniprot/CX7A1_BOVIN CX7A1_BOVIN]] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [[http://www.uniprot.org/uniprot/COX5A_BOVIN COX5A_BOVIN]] This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
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[https://www.uniprot.org/uniprot/COX1_BOVIN COX1_BOVIN] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5x1b" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5x1b" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Cytochrome-c oxidase]]
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[[Category: Large Structures]]
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[[Category: Ago, H]]
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[[Category: Ago H]]
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[[Category: Baba, J]]
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[[Category: Baba J]]
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[[Category: Baba, S]]
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[[Category: Baba S]]
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[[Category: Eto, Y]]
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[[Category: Eto Y]]
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[[Category: Hatano, K]]
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[[Category: Hatano K]]
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[[Category: Hirata, K]]
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[[Category: Hirata K]]
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[[Category: Kimura, T]]
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[[Category: Kimura T]]
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[[Category: Komiya, R]]
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[[Category: Komiya R]]
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[[Category: Kubo, M]]
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[[Category: Kubo M]]
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[[Category: Kumasaka, T]]
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[[Category: Kumasaka T]]
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[[Category: Miyamoto, A]]
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[[Category: Miyamoto A]]
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[[Category: Murakami, H]]
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[[Category: Murakami H]]
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[[Category: Nomura, T]]
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[[Category: Nomura T]]
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[[Category: Ogura, T]]
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[[Category: Ogura T]]
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[[Category: Owada, S]]
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[[Category: Owada S]]
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[[Category: Sakaguchi, M]]
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[[Category: Sakaguchi M]]
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[[Category: Shimada, A]]
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[[Category: Shimada A]]
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[[Category: Shinzawa-Itoh, K]]
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[[Category: Shinzawa-Itoh K]]
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[[Category: Tono, K]]
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[[Category: Tono K]]
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[[Category: Tsukihara, T]]
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[[Category: Tsukihara T]]
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[[Category: Ueno, G]]
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[[Category: Ueno G]]
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[[Category: Yabashi, M]]
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[[Category: Yabashi M]]
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[[Category: Yamaguchi, Y]]
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[[Category: Yamaguchi Y]]
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[[Category: Yamamoto, M]]
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[[Category: Yamamoto M]]
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[[Category: Yamashita, E]]
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[[Category: Yamashita E]]
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[[Category: Yamashita, K]]
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[[Category: Yamashita K]]
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[[Category: Yan, J]]
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[[Category: Yan J]]
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[[Category: Yanagisawa, S]]
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[[Category: Yanagisawa S]]
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[[Category: Yoshikawa, S]]
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[[Category: Yoshikawa S]]
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[[Category: Cytochrome c oxidase]]
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[[Category: Membrane protein]]
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[[Category: Oxidoreductase]]
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[[Category: Proton pump]]
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[[Category: Time-resolved analysis]]
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[[Category: X-ray free electron laser]]
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Current revision

CO bound cytochrome c oxidase at 20 nsec after pump laser irradiation to release CO from O2 reduction center

PDB ID 5x1b

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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