Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006121 | biological_process | mitochondrial electron transport, succinate to ubiquinone |
| A | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031966 | cellular_component | mitochondrial membrane |
| A | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
| A | 0045333 | biological_process | cellular respiration |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
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. CREGICGSC |
| Chain | Residue | Details |
| B | CYS87-CYS95 | |
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCStSCP |
| Chain | Residue | Details |
| B | CYS179-PRO190 | |
| site_id | PS00504 |
| Number of Residues | 10 |
| Details | FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAqGG |
| Chain | Residue | Details |
| A | ARG88-GLY97 | |
| site_id | PS01000 |
| Number of Residues | 25 |
| Details | SDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPIsphLtiyqpqLtwylSsfHRiS |
| Chain | Residue | Details |
| C | ARG75-SER99 | |
| site_id | PS01001 |
| Number of Residues | 14 |
| Details | SDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HyggAIRHLiWDtA |
| Chain | Residue | Details |
| C | HIS156-ALA169 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9YHT1","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9YHT1","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"UniProtKB","id":"Q9YHT1","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 91 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 30 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 120 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 28 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 22 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]} |
