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 | ubiquinol-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 | ubiquinol-cytochrome-c reductase activity |
C | 0016020 | cellular_component | membrane |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0046872 | molecular_function | metal ion 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 | ubiquinol-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 | ubiquinol-cytochrome-c reductase activity |
F | 0016020 | cellular_component | membrane |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0046872 | molecular_function | metal ion 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 | 42 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
C | PHE18-VAL39 | |
A | LEU394-ILE414 | |
D | ILE46-VAL66 | |
D | GLY100-SER120 | |
D | TRP129-LEU149 | |
D | PHE156-ILE176 | |
D | PHE194-TRP214 | |
D | LEU253-TYR273 | |
D | TRP296-VAL315 | |
D | PHE330-ASP350 | |
D | TRP365-ALA385 | |
F | PHE18-VAL39 | |
D | LEU394-ILE414 | |
A | TRP129-LEU149 | |
A | PHE156-ILE176 | |
A | PHE194-TRP214 | |
A | LEU253-TYR273 | |
A | TRP296-VAL315 | |
A | PHE330-ASP350 | |
A | TRP365-ALA385 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 |
Chain | Residue | Details |
C | CYS132 | |
C | HIS134 | |
C | CYS152 | |
C | HIS155 | |
F | CYS132 | |
F | HIS134 | |
F | CYS152 | |
F | HIS155 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
B | HIS86 | |
E | HIS86 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433 |
Chain | Residue | Details |
B | MET210 | |
E | MET210 |