2YIU
X-ray structure of the dimeric cytochrome BC1 complex from the soil bacterium paracoccus denitrificans at 2.7 angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0045275 | cellular_component | respiratory chain complex III |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0020037 | molecular_function | heme binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| C | 0016020 | cellular_component | membrane |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0022904 | biological_process | respiratory electron transport chain |
| D | 0045275 | cellular_component | respiratory chain complex III |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1902600 | biological_process | proton transmembrane transport |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0020037 | molecular_function | heme binding |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| F | 0016020 | cellular_component | membrane |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051536 | molecular_function | iron-sulfur cluster binding |
| F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| F | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | GLN58 |
| A | LEU149 |
| A | PRO150 |
| A | HIS198 |
| A | PRO202 |
| A | GLY62 |
| A | ILE63 |
| A | VAL66 |
| A | ARG94 |
| A | HIS97 |
| A | PHE104 |
| A | THR142 |
| A | GLY146 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | TRP45 |
| A | GLY48 |
| A | LEU51 |
| A | ALA52 |
| A | HIS111 |
| A | ARG114 |
| A | SER120 |
| A | ARG125 |
| A | TRP129 |
| A | GLY132 |
| A | MET133 |
| A | ILE135 |
| A | HIS212 |
| A | PHE216 |
| A | GLY220 |
| A | ASN221 |
| A | ASN222 |
| A | HOH2002 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SMA A 502 |
| Chain | Residue |
| A | LEU137 |
| A | MET154 |
| A | GLY158 |
| A | VAL161 |
| A | PHE194 |
| A | ILE292 |
| A | GLU295 |
| A | PHE298 |
| A | TYR302 |
| A | MET336 |
| A | PHE337 |
| F | CYS154 |
| F | HIS155 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HEC B 500 |
| Chain | Residue |
| B | VAL81 |
| B | CYS82 |
| B | CYS85 |
| B | HIS86 |
| B | PRO145 |
| B | ARG154 |
| B | TYR177 |
| B | LEU182 |
| B | PHE203 |
| B | GLN209 |
| B | MET210 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES C 500 |
| Chain | Residue |
| C | CYS132 |
| C | HIS134 |
| C | LEU135 |
| C | CYS152 |
| C | HIS155 |
| C | SER157 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM D 500 |
| Chain | Residue |
| D | GLN58 |
| D | GLY62 |
| D | ILE63 |
| D | VAL66 |
| D | ARG94 |
| D | HIS97 |
| D | ALA98 |
| D | PHE104 |
| D | GLY146 |
| D | LEU149 |
| D | PRO150 |
| D | HIS198 |
| D | PRO202 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM D 501 |
| Chain | Residue |
| D | TRP45 |
| D | GLY48 |
| D | LEU51 |
| D | ALA52 |
| D | HIS111 |
| D | ARG114 |
| D | SER120 |
| D | ARG125 |
| D | GLY132 |
| D | MET133 |
| D | ILE135 |
| D | VAL209 |
| D | HIS212 |
| D | PHE216 |
| D | GLY220 |
| D | ASN221 |
| D | ASN222 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SMA D 502 |
| Chain | Residue |
| D | PHE298 |
| D | TYR302 |
| D | MET336 |
| D | PHE337 |
| D | ILE340 |
| C | CYS154 |
| C | HIS155 |
| D | LEU137 |
| D | MET140 |
| D | VAL161 |
| D | ILE292 |
| D | PRO294 |
| D | GLU295 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HEC E 500 |
| Chain | Residue |
| E | VAL81 |
| E | CYS82 |
| E | CYS85 |
| E | HIS86 |
| E | ARG154 |
| E | TYR177 |
| E | PHE203 |
| E | GLN209 |
| E | MET210 |
| E | PRO213 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES F 500 |
| Chain | Residue |
| F | CYS132 |
| F | HIS134 |
| F | LEU135 |
| F | CYS152 |
| F | HIS155 |
| F | SER157 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 440 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Note=Anchors to the membrane","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 42 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"covalent"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 186 |
| Details | Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






