2FYN
Crystal Structure Analysis of the double mutant Rhodobacter Sphaeroides bc1 complex
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 | 0005886 | cellular_component | plasma membrane |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion 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 | 0005886 | cellular_component | plasma membrane |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion 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 |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| G | 0009055 | molecular_function | electron transfer activity |
| G | 0016020 | cellular_component | membrane |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0022904 | biological_process | respiratory electron transport chain |
| G | 0045275 | cellular_component | respiratory chain complex III |
| G | 0046872 | molecular_function | metal ion binding |
| G | 1902600 | biological_process | proton transmembrane transport |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0009055 | molecular_function | electron transfer activity |
| H | 0020037 | molecular_function | heme binding |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0005886 | cellular_component | plasma membrane |
| I | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| I | 0016020 | cellular_component | membrane |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0051536 | molecular_function | iron-sulfur cluster binding |
| I | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| I | 1902600 | biological_process | proton transmembrane transport |
| J | 0005886 | cellular_component | plasma membrane |
| J | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| J | 0009055 | molecular_function | electron transfer activity |
| J | 0016020 | cellular_component | membrane |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0022904 | biological_process | respiratory electron transport chain |
| J | 0045275 | cellular_component | respiratory chain complex III |
| J | 0046872 | molecular_function | metal ion binding |
| J | 1902600 | biological_process | proton transmembrane transport |
| K | 0005886 | cellular_component | plasma membrane |
| K | 0009055 | molecular_function | electron transfer activity |
| K | 0020037 | molecular_function | heme binding |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0005886 | cellular_component | plasma membrane |
| L | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| L | 0016020 | cellular_component | membrane |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0051536 | molecular_function | iron-sulfur cluster binding |
| L | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| L | 1902600 | biological_process | proton transmembrane transport |
| M | 0005886 | cellular_component | plasma membrane |
| M | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| M | 0009055 | molecular_function | electron transfer activity |
| M | 0016020 | cellular_component | membrane |
| M | 0016491 | molecular_function | oxidoreductase activity |
| M | 0022904 | biological_process | respiratory electron transport chain |
| M | 0045275 | cellular_component | respiratory chain complex III |
| M | 0046872 | molecular_function | metal ion binding |
| M | 1902600 | biological_process | proton transmembrane transport |
| N | 0005886 | cellular_component | plasma membrane |
| N | 0009055 | molecular_function | electron transfer activity |
| N | 0020037 | molecular_function | heme binding |
| N | 0046872 | molecular_function | metal ion binding |
| O | 0005886 | cellular_component | plasma membrane |
| O | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| O | 0016020 | cellular_component | membrane |
| O | 0046872 | molecular_function | metal ion binding |
| O | 0051536 | molecular_function | iron-sulfur cluster binding |
| O | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| O | 1902600 | biological_process | proton transmembrane transport |
| P | 0005886 | cellular_component | plasma membrane |
| P | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| P | 0009055 | molecular_function | electron transfer activity |
| P | 0016020 | cellular_component | membrane |
| P | 0016491 | molecular_function | oxidoreductase activity |
| P | 0022904 | biological_process | respiratory electron transport chain |
| P | 0045275 | cellular_component | respiratory chain complex III |
| P | 0046872 | molecular_function | metal ion binding |
| P | 1902600 | biological_process | proton transmembrane transport |
| Q | 0005886 | cellular_component | plasma membrane |
| Q | 0009055 | molecular_function | electron transfer activity |
| Q | 0020037 | molecular_function | heme binding |
| Q | 0046872 | molecular_function | metal ion binding |
| R | 0005886 | cellular_component | plasma membrane |
| R | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| R | 0016020 | cellular_component | membrane |
| R | 0046872 | molecular_function | metal ion binding |
| R | 0051536 | molecular_function | iron-sulfur cluster binding |
| R | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| R | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | TRP45 |
| A | TRP129 |
| A | GLY132 |
| A | MET133 |
| A | ILE135 |
| A | TYR136 |
| A | VAL209 |
| A | HIS212 |
| A | PHE216 |
| A | THR219 |
| A | GLY220 |
| A | GLY48 |
| A | ASN222 |
| A | LEU51 |
| A | ALA52 |
| A | VAL108 |
| A | HIS111 |
| A | ARG114 |
| A | ARG125 |
| A | THR128 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM A 502 |
| Chain | Residue |
| A | GLN58 |
| A | ILE59 |
| A | GLY62 |
| A | ILE63 |
| A | LEU65 |
| A | ARG94 |
| A | HIS97 |
| A | ALA98 |
| A | THR142 |
| A | GLY146 |
| A | LEU149 |
| A | PRO150 |
| A | HIS198 |
| A | TYR199 |
| A | PRO202 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM B 301 |
| Chain | Residue |
| B | VAL35 |
| B | CYS36 |
| B | CYS39 |
| B | HIS40 |
| B | LEU94 |
| B | ASN96 |
| B | PRO98 |
| B | MET103 |
| B | ARG107 |
| B | TYR130 |
| B | ALA184 |
| B | MET185 |
| B | PRO188 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES C 200 |
| Chain | Residue |
| C | CYS129 |
| C | HIS131 |
| C | LEU132 |
| C | GLY133 |
| C | CYS149 |
| C | HIS152 |
| C | SER154 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM D 501 |
| Chain | Residue |
| D | TRP45 |
| D | GLY48 |
| D | LEU51 |
| D | ALA52 |
| D | VAL108 |
| D | HIS111 |
| D | ARG114 |
| D | ARG125 |
| D | THR128 |
| D | TRP129 |
| D | GLY132 |
| D | MET133 |
| D | ILE135 |
| D | TYR136 |
| D | VAL209 |
| D | HIS212 |
| D | PHE216 |
| D | GLY220 |
| D | ASN221 |
| D | ASN222 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM D 502 |
| Chain | Residue |
| D | GLN58 |
| D | GLY62 |
| D | ILE63 |
| D | ARG94 |
| D | HIS97 |
| D | THR142 |
| D | ALA143 |
| D | GLY146 |
| D | TYR147 |
| D | LEU149 |
| D | PRO150 |
| D | HIS198 |
| D | TYR199 |
| D | PRO202 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM E 301 |
| Chain | Residue |
| E | LEU135 |
| E | PHE160 |
| E | ILE183 |
| E | MET185 |
| E | PRO188 |
| E | VAL35 |
| E | CYS36 |
| E | CYS39 |
| E | HIS40 |
| E | LEU94 |
| E | ASN96 |
| E | PRO98 |
| E | MET103 |
| E | ARG107 |
| E | TYR130 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES F 200 |
| Chain | Residue |
| F | CYS129 |
| F | HIS131 |
| F | LEU132 |
| F | GLY133 |
| F | CYS149 |
| F | HIS152 |
| F | SER154 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM G 501 |
| Chain | Residue |
| G | TRP45 |
| G | GLY48 |
| G | LEU51 |
| G | ALA52 |
| G | VAL108 |
| G | HIS111 |
| G | ILE112 |
| G | ARG114 |
| G | ARG125 |
| G | THR128 |
| G | TRP129 |
| G | GLY132 |
| G | MET133 |
| G | ILE135 |
| G | TYR136 |
| G | VAL209 |
| G | HIS212 |
| G | PHE216 |
| G | ASN222 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM G 502 |
| Chain | Residue |
| G | GLN58 |
| G | GLY62 |
| G | ILE63 |
| G | VAL80 |
| G | ARG94 |
| G | HIS97 |
| G | THR142 |
| G | ALA143 |
| G | GLY146 |
| G | TYR147 |
| G | PRO150 |
| G | HIS198 |
| G | TYR199 |
| G | PRO202 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM H 301 |
| Chain | Residue |
| H | VAL35 |
| H | CYS36 |
| H | CYS39 |
| H | HIS40 |
| H | ASN96 |
| H | PRO98 |
| H | MET103 |
| H | ARG107 |
| H | TYR130 |
| H | ILE183 |
| H | ALA184 |
| H | MET185 |
| H | PRO188 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES I 200 |
| Chain | Residue |
| I | CYS129 |
| I | HIS131 |
| I | LEU132 |
| I | GLY133 |
| I | CYS134 |
| I | CYS149 |
| I | HIS152 |
| I | SER154 |
| site_id | BC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM J 501 |
| Chain | Residue |
| J | TRP45 |
| J | GLY48 |
| J | LEU51 |
| J | ALA52 |
| J | VAL108 |
| J | HIS111 |
| J | ARG114 |
| J | ARG125 |
| J | THR128 |
| J | TRP129 |
| J | GLY132 |
| J | MET133 |
| J | ILE135 |
| J | TYR136 |
| J | VAL209 |
| J | HIS212 |
| J | PHE216 |
| J | GLY220 |
| J | ASN222 |
| site_id | BC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM J 502 |
| Chain | Residue |
| J | GLN58 |
| J | GLY62 |
| J | ILE63 |
| J | ARG94 |
| J | HIS97 |
| J | ALA101 |
| J | THR142 |
| J | GLY146 |
| J | TYR147 |
| J | PRO150 |
| J | HIS198 |
| J | TYR199 |
| J | PRO202 |
| site_id | BC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM K 301 |
| Chain | Residue |
| K | VAL35 |
| K | CYS36 |
| K | CYS39 |
| K | HIS40 |
| K | ASN96 |
| K | PRO98 |
| K | MET103 |
| K | ARG107 |
| K | TYR130 |
| K | LEU135 |
| K | ILE183 |
| K | ALA184 |
| K | MET185 |
| K | PRO188 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES L 200 |
| Chain | Residue |
| L | CYS129 |
| L | HIS131 |
| L | LEU132 |
| L | GLY133 |
| L | CYS134 |
| L | CYS149 |
| L | HIS152 |
| L | SER154 |
| site_id | BC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM M 501 |
| Chain | Residue |
| M | TRP45 |
| M | GLY48 |
| M | LEU51 |
| M | ALA52 |
| M | VAL108 |
| M | HIS111 |
| M | ILE112 |
| M | ARG114 |
| M | SER120 |
| M | ARG125 |
| M | TRP129 |
| M | GLY132 |
| M | MET133 |
| M | ILE135 |
| M | TYR136 |
| M | VAL209 |
| M | HIS212 |
| M | PHE216 |
| M | ASN221 |
| M | ASN222 |
| site_id | BC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM M 502 |
| Chain | Residue |
| M | GLN58 |
| M | GLY62 |
| M | ILE63 |
| M | ARG94 |
| M | HIS97 |
| M | ALA98 |
| M | THR142 |
| M | GLY146 |
| M | LEU149 |
| M | PRO150 |
| M | PHE195 |
| M | HIS198 |
| M | TYR199 |
| M | PRO202 |
| site_id | CC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM N 301 |
| Chain | Residue |
| N | VAL35 |
| N | CYS36 |
| N | CYS39 |
| N | HIS40 |
| N | LEU94 |
| N | ASN96 |
| N | PRO98 |
| N | ARG107 |
| N | ILE131 |
| N | LEU135 |
| N | PHE160 |
| N | ILE183 |
| N | ALA184 |
| N | MET185 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES O 200 |
| Chain | Residue |
| O | CYS129 |
| O | HIS131 |
| O | LEU132 |
| O | GLY133 |
| O | CYS149 |
| O | HIS152 |
| O | SER154 |
| site_id | CC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM P 501 |
| Chain | Residue |
| P | TRP45 |
| P | GLY48 |
| P | LEU51 |
| P | ALA52 |
| P | VAL108 |
| P | HIS111 |
| P | ARG114 |
| P | SER120 |
| P | ARG125 |
| P | THR128 |
| P | TRP129 |
| P | GLY132 |
| P | MET133 |
| P | ILE135 |
| P | TYR136 |
| P | VAL209 |
| P | HIS212 |
| P | PHE216 |
| P | THR219 |
| P | ASN221 |
| P | ASN222 |
| site_id | CC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM P 502 |
| Chain | Residue |
| P | GLN58 |
| P | GLY62 |
| P | ILE63 |
| P | LEU65 |
| P | ARG94 |
| P | HIS97 |
| P | ALA101 |
| P | THR142 |
| P | GLY146 |
| P | TYR147 |
| P | LEU149 |
| P | PRO150 |
| P | HIS198 |
| P | TYR199 |
| P | PRO202 |
| site_id | CC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM Q 301 |
| Chain | Residue |
| Q | VAL35 |
| Q | CYS36 |
| Q | CYS39 |
| Q | HIS40 |
| Q | LEU94 |
| Q | ASN96 |
| Q | PRO98 |
| Q | MET103 |
| Q | ARG107 |
| Q | TYR130 |
| Q | ILE131 |
| Q | LEU135 |
| Q | ILE183 |
| Q | ALA184 |
| Q | MET185 |
| Q | PRO188 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES R 200 |
| Chain | Residue |
| R | CYS129 |
| R | HIS131 |
| R | LEU132 |
| R | GLY133 |
| R | CYS149 |
| R | HIS152 |
| R | SER154 |
| site_id | CC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SMA A 503 |
| Chain | Residue |
| A | PHE144 |
| A | GLY158 |
| A | VAL161 |
| A | ILE162 |
| A | ILE292 |
| A | VAL293 |
| A | PRO294 |
| A | GLU295 |
| A | PHE298 |
| A | PHE301 |
| A | TYR302 |
| A | PHE337 |
| A | ILE340 |
| F | CYS151 |
| F | HIS152 |
| site_id | CC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SMA D 503 |
| Chain | Residue |
| C | CYS151 |
| C | HIS152 |
| D | MET140 |
| D | GLY158 |
| D | VAL161 |
| D | ILE162 |
| D | ILE292 |
| D | PRO294 |
| D | GLU295 |
| D | PHE298 |
| D | TYR302 |
| D | MET336 |
| D | PHE337 |
| site_id | CC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SMA G 503 |
| Chain | Residue |
| G | PHE144 |
| G | GLY158 |
| G | VAL161 |
| G | ILE162 |
| G | PHE194 |
| G | ILE292 |
| G | VAL293 |
| G | PRO294 |
| G | GLU295 |
| G | PHE298 |
| G | TYR302 |
| G | PHE337 |
| L | HIS152 |
| site_id | DC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SMA J 503 |
| Chain | Residue |
| I | CYS151 |
| I | HIS152 |
| J | MET140 |
| J | PHE144 |
| J | GLY158 |
| J | VAL161 |
| J | ILE162 |
| J | ILE292 |
| J | VAL293 |
| J | PRO294 |
| J | GLU295 |
| J | PHE298 |
| J | TYR302 |
| J | MET336 |
| site_id | DC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SMA M 503 |
| Chain | Residue |
| M | PHE144 |
| M | GLY158 |
| M | VAL161 |
| M | ILE162 |
| M | PHE194 |
| M | VAL293 |
| M | PRO294 |
| M | GLU295 |
| M | PHE298 |
| M | TYR302 |
| R | HIS152 |
| site_id | DC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SMA P 503 |
| Chain | Residue |
| O | CYS151 |
| O | HIS152 |
| P | MET145 |
| P | GLY158 |
| P | VAL161 |
| P | ILE162 |
| P | LEU180 |
| P | ILE292 |
| P | PRO294 |
| P | GLU295 |
| P | PHE298 |
| P | TYR302 |
| P | MET336 |
| P | PHE337 |
| site_id | DC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LOP A 504 |
| Chain | Residue |
| A | MET44 |
| A | TYR117 |
| A | TYR118 |
| A | PHE263 |
| A | ARG358 |
| A | PHE374 |
| site_id | DC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LOP D 504 |
| Chain | Residue |
| D | PHE113 |
| D | ARG114 |
| D | TYR117 |
| D | TYR118 |
| D | LEU274 |
| D | ARG358 |
| D | TRP368 |
| D | PHE374 |
| site_id | DC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LOP G 504 |
| Chain | Residue |
| G | MET44 |
| G | TRP47 |
| G | ASN99 |
| G | LEU103 |
| G | ILE106 |
| G | PHE113 |
| G | TYR117 |
| G | TYR118 |
| G | ARG358 |
| site_id | DC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LOP J 504 |
| Chain | Residue |
| J | MET44 |
| J | PHE113 |
| J | TYR117 |
| J | TYR118 |
| J | VAL262 |
| J | PHE263 |
| J | ARG358 |
| J | PHE374 |
| site_id | DC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LOP M 504 |
| Chain | Residue |
| M | MET44 |
| M | PHE113 |
| M | TYR117 |
| M | TYR118 |
| M | ARG358 |
| M | PHE374 |
| site_id | DC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LOP P 504 |
| Chain | Residue |
| P | PHE113 |
| P | TYR117 |
| P | TYR118 |
| P | LEU274 |
| P | ARG358 |
| P | TRP368 |
| P | PHE374 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 870 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 792 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 402 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 30 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 108 |
| Details | Transmembrane: {"description":"Helical; Note=Anchors to the membrane","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"covalent"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 120 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 576 |
| Details | Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| F | HIS152 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| O | HIS152 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| I | HIS152 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| R | HIS152 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| C | HIS152 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| L | HIS152 |
