2ACZ
Complex II (Succinate Dehydrogenase) From E. Coli with Atpenin A5 inhibitor co-crystallized at the ubiquinone binding site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000104 | molecular_function | succinate dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009060 | biological_process | aerobic respiration |
| A | 0009061 | biological_process | anaerobic respiration |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0019646 | biological_process | aerobic electron transport chain |
| A | 0022900 | biological_process | electron transport chain |
| A | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009060 | biological_process | aerobic respiration |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019646 | biological_process | aerobic electron transport chain |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
| 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 |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0009060 | biological_process | aerobic respiration |
| C | 0016020 | cellular_component | membrane |
| C | 0017004 | biological_process | cytochrome complex assembly |
| C | 0019646 | biological_process | aerobic electron transport chain |
| C | 0020037 | molecular_function | heme binding |
| C | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048039 | molecular_function | ubiquinone binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0009060 | biological_process | aerobic respiration |
| D | 0016020 | cellular_component | membrane |
| D | 0017004 | biological_process | cytochrome complex assembly |
| D | 0019646 | biological_process | aerobic electron transport chain |
| D | 0020037 | molecular_function | heme binding |
| D | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OAA A 589 |
| Chain | Residue |
| A | GLY51 |
| A | GLY401 |
| A | GLY402 |
| A | FAD601 |
| A | PHE126 |
| A | HIS242 |
| A | LEU252 |
| A | THR254 |
| A | GLU255 |
| A | ARG286 |
| A | HIS354 |
| A | ARG399 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 601 |
| Chain | Residue |
| A | GLY14 |
| A | ALA15 |
| A | GLY16 |
| A | GLY17 |
| A | ALA18 |
| A | SER37 |
| A | LYS38 |
| A | VAL39 |
| A | SER44 |
| A | HIS45 |
| A | THR46 |
| A | SER48 |
| A | ALA49 |
| A | GLN50 |
| A | GLY51 |
| A | GLY52 |
| A | TRP164 |
| A | TYR165 |
| A | ALA166 |
| A | ALA201 |
| A | THR202 |
| A | GLY203 |
| A | ASN214 |
| A | ASP221 |
| A | TYR355 |
| A | GLU388 |
| A | ARG399 |
| A | GLY402 |
| A | SER404 |
| A | LEU405 |
| A | LEU408 |
| A | OAA589 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES B 302 |
| Chain | Residue |
| B | SER54 |
| B | CYS55 |
| B | ARG56 |
| B | GLY58 |
| B | VAL59 |
| B | CYS60 |
| B | GLY61 |
| B | ASP63 |
| B | CYS75 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 303 |
| Chain | Residue |
| B | CYS149 |
| B | ILE150 |
| B | CYS152 |
| B | ALA153 |
| B | CYS154 |
| B | CYS155 |
| B | CYS216 |
| B | PRO217 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE F3S B 304 |
| Chain | Residue |
| B | CYS159 |
| B | PRO172 |
| B | CYS206 |
| B | HIS207 |
| B | SER208 |
| B | ILE209 |
| B | MET210 |
| B | ASN211 |
| B | CYS212 |
| B | THR223 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEB C 130 |
| Chain | Residue |
| B | HIS207 |
| C | HIS30 |
| C | ARG31 |
| C | THR37 |
| C | PHE38 |
| C | HIS84 |
| C | VAL85 |
| C | GLY88 |
| C | CDN132 |
| D | ARG20 |
| D | ALA23 |
| D | THR27 |
| D | ILE68 |
| D | HIS71 |
| D | GLY75 |
| D | MET76 |
| D | GLN78 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AT5 C 131 |
| Chain | Residue |
| D | TYR83 |
| B | PRO160 |
| B | TRP164 |
| B | HIS207 |
| B | ILE209 |
| C | LEU15 |
| C | PHE20 |
| C | ALA24 |
| C | SER27 |
| C | ILE28 |
| C | ARG31 |
| D | ASP82 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CDN C 132 |
| Chain | Residue |
| C | LEU44 |
| C | SER51 |
| C | ALA61 |
| C | SER62 |
| C | MET65 |
| C | MET74 |
| C | LEU78 |
| C | VAL115 |
| C | LEU123 |
| C | ALA124 |
| C | VAL126 |
| C | LEU127 |
| C | TRP129 |
| C | HEB130 |
| D | ILE30 |
| D | GLY41 |
| D | LEU43 |
| D | ILE68 |
Functional Information from PROSITE/UniProt
| 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 | CYS149-PRO160 |
| site_id | PS00504 |
| Number of Residues | 10 |
| Details | FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvsAqGG |
| Chain | Residue | Details |
| A | ARG43-GLY52 |
| site_id | PS01000 |
| Number of Residues | 25 |
| Details | SDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPVnldLqtirfpItaiaSilHRvS |
| Chain | Residue | Details |
| C | ARG9-SER33 |
| site_id | PS01001 |
| Number of Residues | 14 |
| Details | SDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HvvvGIRHMmMDfG |
| Chain | Residue | Details |
| C | HIS84-GLY97 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19710024","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 23 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12560550","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16407191","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19710024","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19710024","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":"12560550","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16407191","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19710024","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 89 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| 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_FI8 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12560550","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 43 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 130 |
| Details | Transmembrane: {"description":"Helical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 15 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 21 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 9 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d4c |
| Chain | Residue | Details |
| A | HIS242 | |
| A | ARG286 | |
| A | HIS354 | |
| A | ARG399 |
