3EHB
A D-Pathway Mutation Decouples the Paracoccus Denitrificans Cytochrome c Oxidase by Altering the side chain orientation of a distant, conserved Glutamate
Summary for 3EHB
Entry DOI | 10.2210/pdb3ehb/pdb |
Related | 1AR1 |
Descriptor | Cytochrome c oxidase subunit 1-beta, DODECYL-BETA-D-MALTOSIDE, PEROXIDE ION, ... (12 entities in total) |
Functional Keywords | proton pumping, water chain, electron transfer, cell inner membrane, cell membrane, copper, electron transport, heme, hydrogen ion transport, ion transport, iron, membrane, metal-binding, oxidoreductase, respiratory chain, transmembrane, transport, pyrrolidone carboxylic acid, oxidoreductase-immune system complex, oxidoreductase/immune system |
Biological source | Paracoccus denitrificans More |
Cellular location | Cell inner membrane; Multi-pass membrane protein: P98002 P08306 |
Total number of polymer chains | 4 |
Total formula weight | 132821.68 |
Authors | Koepke, J.,Mueller, H.,Peng, G. (deposition date: 2008-09-12, release date: 2008-09-30, Last modification date: 2023-11-01) |
Primary citation | Durr, K.L.,Koepke, J.,Hellwig, P.,Muller, H.,Angerer, H.,Peng, G.,Olkhova, E.,Richter, O.-M.H.,Ludwig, B.,Michel, H. A d-pathway mutation decouples the paracoccusdenitrificans cytochrome C oxidase by altering the side-chain orientation of a distant conserved glutamate J.Mol.Biol., 384:865-877, 2008 Cited by PubMed: 18930738DOI: 10.1016/j.jmb.2008.09.074 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.32 Å) |
Structure validation
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