1YQ4
Avian respiratory complex ii with 3-nitropropionate and ubiquinone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006105 | biological_process | succinate metabolic process |
| 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 | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0022900 | biological_process | electron transport chain |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016020 | cellular_component | membrane |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005740 | cellular_component | mitochondrial envelope |
| D | 0016020 | cellular_component | membrane |
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 | CYS65-CYS73 |
| 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 | CYS158-PRO169 |
| site_id | PS00504 |
| Number of Residues | 10 |
| Details | FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAqGG |
| Chain | Residue | Details |
| A | ARG54-GLY63 |
| site_id | PS01000 |
| Number of Residues | 25 |
| Details | SDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPLsphIsiykwsLpmamSitHRgT |
| Chain | Residue | Details |
| C | ARG21-THR45 |
| site_id | PS01001 |
| Number of Residues | 14 |
| Details | SDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtwnGIRHLvWDmG |
| Chain | Residue | Details |
| C | HIS98-GLY111 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15805592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 93 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 30 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YQ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H88","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 62 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 20 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YQ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YQ4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FBW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H88","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H89","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 294 |
| Chain | Residue | Details |
| A | PHE130 | steric role |
| A | GLN251 | electrostatic stabiliser, hydrogen bond acceptor, steric role |
| A | HIS253 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | LEU263 | steric role |
| A | GLU266 | electrostatic stabiliser, hydrogen bond acceptor, steric role |
| A | ARG297 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS364 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | ARG408 | electrostatic stabiliser, hydrogen bond donor, steric role |
