Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0022900 | biological_process | electron transport chain |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0070469 | cellular_component | respirasome |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0070469 | cellular_component | respirasome |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0016020 | cellular_component | membrane |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070469 | cellular_component | respirasome |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0022900 | biological_process | electron transport chain |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0070469 | cellular_component | respirasome |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0006099 | biological_process | tricarboxylic acid cycle |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| E | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| E | 0070469 | cellular_component | respirasome |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0006099 | biological_process | tricarboxylic acid cycle |
| F | 0016020 | cellular_component | membrane |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0070469 | cellular_component | respirasome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1658 |
| Chain | Residue |
| A | SER371 |
| A | MET372 |
| A | GLY373 |
| A | GLU393 |
| A | ALA395 |
| A | HOH2158 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 1658 |
| Chain | Residue |
| D | GLU393 |
| D | ALA395 |
| D | HOH2156 |
| D | SER371 |
| D | MET372 |
| D | GLY373 |
| site_id | AC3 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD A 1656 |
| Chain | Residue |
| A | GLY12 |
| A | GLY13 |
| A | GLY14 |
| A | LEU15 |
| A | ALA16 |
| A | SER35 |
| A | LEU36 |
| A | ILE37 |
| A | SER42 |
| A | HIS43 |
| A | SER44 |
| A | ALA47 |
| A | GLY49 |
| A | GLY50 |
| A | LYS179 |
| A | GLU180 |
| A | ALA181 |
| A | ALA215 |
| A | THR216 |
| A | GLY217 |
| A | THR227 |
| A | ASN228 |
| A | THR235 |
| A | LEU267 |
| A | HIS369 |
| A | TYR370 |
| A | GLY392 |
| A | GLU393 |
| A | ARG404 |
| A | GLY407 |
| A | ASN408 |
| A | SER409 |
| A | VAL410 |
| A | FUM1657 |
| A | HOH2111 |
| A | HOH2270 |
| A | HOH2271 |
| A | HOH2272 |
| A | HOH2273 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FUM A 1657 |
| Chain | Residue |
| A | GLY49 |
| A | PHE141 |
| A | HIS257 |
| A | LEU267 |
| A | THR269 |
| A | GLU270 |
| A | ARG301 |
| A | HIS369 |
| A | ARG404 |
| A | FAD1656 |
| A | HOH2019 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES B 1240 |
| Chain | Residue |
| B | VAL56 |
| B | CYS57 |
| B | ARG58 |
| B | GLY60 |
| B | ILE61 |
| B | CYS62 |
| B | GLY63 |
| B | CYS65 |
| B | CYS77 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F3S B 1241 |
| Chain | Residue |
| B | CYS161 |
| B | THR163 |
| B | CYS208 |
| B | MET209 |
| B | THR210 |
| B | LEU211 |
| B | LEU212 |
| B | ALA213 |
| B | CYS214 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 B 1242 |
| Chain | Residue |
| B | CYS151 |
| B | ILE152 |
| B | GLU153 |
| B | CYS154 |
| B | GLY155 |
| B | CYS157 |
| B | CYS218 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM C 1255 |
| Chain | Residue |
| C | MET136 |
| C | PHE137 |
| C | HIS182 |
| C | GLY186 |
| C | LEU190 |
| C | LYS193 |
| C | HOH2036 |
| C | HOH2054 |
| C | HOH2055 |
| C | GLN30 |
| C | SER31 |
| C | GLY34 |
| C | LEU37 |
| C | PHE90 |
| C | HIS93 |
| C | ALA94 |
| C | ALA97 |
| C | LYS100 |
| C | PHE101 |
| C | TRP126 |
| C | GLY133 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM C 1256 |
| Chain | Residue |
| C | PHE40 |
| C | MET41 |
| C | HIS44 |
| C | MET45 |
| C | LEU82 |
| C | HIS143 |
| C | MET147 |
| C | ILE154 |
| C | SER159 |
| C | ARG162 |
| C | TYR172 |
| C | LEU176 |
| C | GLY224 |
| C | PHE228 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMT C 1257 |
| Chain | Residue |
| C | PRO102 |
| C | ASN104 |
| C | TYR108 |
| C | MET131 |
| F | PHE95 |
| F | MET98 |
| F | ARG99 |
| site_id | BC2 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD D 1656 |
| Chain | Residue |
| D | GLY12 |
| D | GLY13 |
| D | GLY14 |
| D | LEU15 |
| D | ALA16 |
| D | SER35 |
| D | LEU36 |
| D | ILE37 |
| D | SER42 |
| D | HIS43 |
| D | SER44 |
| D | ALA47 |
| D | GLY49 |
| D | GLY50 |
| D | LYS179 |
| D | GLU180 |
| D | ALA181 |
| D | ALA215 |
| D | THR216 |
| D | GLY217 |
| D | THR227 |
| D | ASN228 |
| D | THR235 |
| D | LEU267 |
| D | HIS369 |
| D | TYR370 |
| D | GLU393 |
| D | ARG404 |
| D | GLY407 |
| D | ASN408 |
| D | SER409 |
| D | VAL410 |
| D | FUM1657 |
| D | HOH2282 |
| D | HOH2283 |
| D | HOH2284 |
| D | HOH2285 |
| D | HOH2286 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FUM D 1657 |
| Chain | Residue |
| D | GLY49 |
| D | PHE141 |
| D | HIS257 |
| D | LEU267 |
| D | THR269 |
| D | GLU270 |
| D | ARG301 |
| D | HIS369 |
| D | ARG404 |
| D | FAD1656 |
| D | HOH2287 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES E 1240 |
| Chain | Residue |
| E | VAL56 |
| E | CYS57 |
| E | ARG58 |
| E | GLY60 |
| E | ILE61 |
| E | CYS62 |
| E | GLY63 |
| E | CYS65 |
| E | CYS77 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F3S E 1241 |
| Chain | Residue |
| E | CYS161 |
| E | THR163 |
| E | CYS208 |
| E | MET209 |
| E | THR210 |
| E | LEU211 |
| E | LEU212 |
| E | ALA213 |
| E | CYS214 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 E 1242 |
| Chain | Residue |
| E | CYS151 |
| E | ILE152 |
| E | GLU153 |
| E | CYS154 |
| E | GLY155 |
| E | CYS157 |
| E | CYS218 |
| E | PRO219 |
| site_id | BC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM F 1255 |
| Chain | Residue |
| F | GLN30 |
| F | SER31 |
| F | GLY34 |
| F | LEU37 |
| F | PHE90 |
| F | HIS93 |
| F | ALA94 |
| F | ALA97 |
| F | LYS100 |
| F | PHE101 |
| F | TRP126 |
| F | GLY133 |
| F | MET136 |
| F | PHE137 |
| F | HIS182 |
| F | GLY186 |
| F | LEU190 |
| F | LYS193 |
| F | HOH2054 |
| F | HOH2055 |
| F | HOH2056 |
| site_id | BC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM F 1256 |
| Chain | Residue |
| F | PHE40 |
| F | MET41 |
| F | HIS44 |
| F | MET45 |
| F | LEU82 |
| F | HIS143 |
| F | MET147 |
| F | ILE154 |
| F | SER159 |
| F | ARG162 |
| F | TYR172 |
| F | LEU176 |
| F | GLY224 |
| F | PHE228 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LMT F 1257 |
| Chain | Residue |
| C | LEU26 |
| C | PHE95 |
| C | MET98 |
| C | ARG99 |
| F | PRO102 |
| F | ASN104 |
| F | TYR108 |
| F | MET131 |
Functional Information from PROSITE/UniProt
| site_id | PS00197 |
| Number of Residues | 9 |
| Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGICGSC |
| Chain | Residue | Details |
| B | CYS57-CYS65 |
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiECGcCIaACG |
| Chain | Residue | Details |
| B | CYS151-GLY162 |
| site_id | PS00504 |
| Number of Residues | 10 |
| Details | FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHSaaAqGG |
| Chain | Residue | Details |
| A | ARG41-GLY50 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10586875 |
| Chain | Residue | Details |
| C | MET1-GLN30 | |
| B | CYS214 | |
| B | CYS218 | |
| E | CYS57 | |
| E | CYS62 | |
| E | CYS65 | |
| E | CYS77 | |
| E | CYS151 | |
| E | CYS154 | |
| E | CYS157 | |
| E | CYS161 | |
| F | MET1-GLN30 | |
| E | CYS208 | |
| E | CYS214 | |
| E | CYS218 | |
| B | CYS65 | |
| B | CYS77 | |
| B | CYS151 | |
| B | CYS154 | |
| B | CYS157 | |
| B | CYS161 | |
| B | CYS208 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 222 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| C | SER31-LEU52 | |
| F | ALA207-ALA230 | |
| C | ILE77-MET98 | |
| C | LEU125-THR149 | |
| C | GLU166-TYR188 | |
| C | ALA207-ALA230 | |
| F | SER31-LEU52 | |
| F | ILE77-MET98 | |
| F | LEU125-THR149 | |
| F | GLU166-TYR188 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 76 |
| Details | TOPO_DOM: Periplasmic |
| Chain | Residue | Details |
| C | LEU53-PRO76 | |
| C | GLN150-SER165 | |
| F | LEU53-PRO76 | |
| F | GLN150-SER165 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 84 |
| Details | TOPO_DOM: Cytoplasmic |
| Chain | Residue | Details |
| C | ARG99-THR124 | |
| C | ARG189-ARG206 | |
| F | ARG99-THR124 | |
| F | ARG189-ARG206 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P, ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2, ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4 |
| Chain | Residue | Details |
| C | HIS44 | |
| C | HIS93 | |
| C | HIS143 | |
| C | HIS182 | |
| F | HIS44 | |
| F | HIS93 | |
| F | HIS143 | |
| F | HIS182 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d4c |
| Chain | Residue | Details |
| A | HIS257 | |
| A | ARG404 | |
| A | HIS369 | |
| A | ARG301 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d4c |
| Chain | Residue | Details |
| D | HIS257 | |
| D | ARG404 | |
| D | HIS369 | |
| D | ARG301 |
