3hb3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:17, 27 November 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase==
==High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase==
-
<StructureSection load='3hb3' size='340' side='right' caption='[[3hb3]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+
<StructureSection load='3hb3' size='340' side='right'caption='[[3hb3]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3hb3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HB3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HB3 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3hb3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HB3 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</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]] 2.25&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ar1|1ar1]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ctaDII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741]), ctaC, coiI, ctaB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741])</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=3hb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hb3 OCA], [https://pdbe.org/3hb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hb3 RCSB], [https://www.ebi.ac.uk/pdbsum/3hb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hb3 ProSAT]</span></td></tr>
-
<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>
+
-
<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=3hb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hb3 OCA], [http://pdbe.org/3hb3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hb3 RCSB], [http://www.ebi.ac.uk/pdbsum/3hb3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hb3 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/COX1B_PARDE COX1B_PARDE]] Subunit I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. [[http://www.uniprot.org/uniprot/COX2_PARDE COX2_PARDE]] Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
+
[https://www.uniprot.org/uniprot/COX1B_PARDE COX1B_PARDE] Subunit I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 17: Line 15:
<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hb/3hb3_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hb/3hb3_consurf.spt"</scriptWhenChecked>
-
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
Line 34: Line 32:
==See Also==
==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Antibody 3D structures|Antibody 3D structures]]
-
*[[Cytochrome c oxidase|Cytochrome c oxidase]]
+
*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
 +
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Atcc 17741]]
+
[[Category: Large Structures]]
-
[[Category: Cytochrome-c oxidase]]
+
[[Category: Mus musculus]]
-
[[Category: Lk3 transgenic mice]]
+
[[Category: Paracoccus denitrificans]]
-
[[Category: Angerer, H]]
+
[[Category: Angerer H]]
-
[[Category: Koepke, J]]
+
[[Category: Koepke J]]
-
[[Category: Peng, G]]
+
[[Category: Peng G]]
-
[[Category: Cell inner membrane]]
+
-
[[Category: Cell membrane]]
+
-
[[Category: Copper]]
+
-
[[Category: Disulfide bond]]
+
-
[[Category: Electron transfer]]
+
-
[[Category: Electron transport]]
+
-
[[Category: Heme]]
+
-
[[Category: Hydrogen ion transport]]
+
-
[[Category: Ion transport]]
+
-
[[Category: Iron]]
+
-
[[Category: Membrane]]
+
-
[[Category: Membrane protein]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Proton pumping]]
+
-
[[Category: Proton transfer]]
+
-
[[Category: Pyrrolidone carboxylic acid]]
+
-
[[Category: Respiratory chain]]
+
-
[[Category: Transmembrane]]
+
-
[[Category: Transport]]
+

Current revision

High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase

PDB ID 3hb3

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/3hb3"
Personal tools