3AEG
Crystal structure of porcine heart mitochondrial complex II bound with N-Biphenyl-3-yl-2-iodo-benzamide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005739 | cellular_component | mitochondrion |
| 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 | 0007399 | biological_process | nervous system development |
| 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 | 0005515 | molecular_function | protein binding |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006121 | biological_process | mitochondrial electron transport, succinate to ubiquinone |
| B | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009060 | biological_process | aerobic respiration |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0031966 | cellular_component | mitochondrial membrane |
| B | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048039 | molecular_function | ubiquinone 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 | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016020 | cellular_component | membrane |
| D | 0005740 | cellular_component | mitochondrial envelope |
| D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 700 |
| Chain | Residue |
| A | GLY26 |
| A | SER56 |
| A | HIS57 |
| A | THR58 |
| A | ALA60 |
| A | ALA61 |
| A | GLN62 |
| A | GLY63 |
| A | GLY64 |
| A | TYR177 |
| A | PHE178 |
| A | ALA27 |
| A | ALA179 |
| A | ALA213 |
| A | THR214 |
| A | GLY215 |
| A | ASP233 |
| A | LEU264 |
| A | HIS365 |
| A | GLU398 |
| A | ARG409 |
| A | ALA412 |
| A | GLY28 |
| A | SER414 |
| A | LEU415 |
| A | LEU418 |
| A | GLY29 |
| A | ALA30 |
| A | VAL48 |
| A | THR49 |
| A | LYS50 |
| A | LEU51 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES B 302 |
| Chain | Residue |
| B | CYS65 |
| B | ARG66 |
| B | GLY68 |
| B | CYS70 |
| B | GLY71 |
| B | CYS73 |
| B | CYS85 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 303 |
| Chain | Residue |
| B | CYS158 |
| B | ILE159 |
| B | CYS161 |
| B | ALA162 |
| B | CYS164 |
| B | ALA182 |
| B | CYS225 |
| B | PRO226 |
| B | PRO231 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F3S B 304 |
| Chain | Residue |
| B | CYS168 |
| B | TYR178 |
| B | PRO181 |
| B | CYS215 |
| B | ILE218 |
| B | MET219 |
| B | CYS221 |
| B | GLY232 |
| B | ILE235 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM C 1305 |
| Chain | Residue |
| C | HIS45 |
| C | ARG46 |
| C | GLY49 |
| C | LEU52 |
| C | SER53 |
| C | VAL56 |
| C | HIS101 |
| C | THR102 |
| C | GLY105 |
| C | HIS108 |
| D | ARG47 |
| D | SER50 |
| D | LEU53 |
| D | LEU54 |
| D | LEU57 |
| D | HIS79 |
| D | GLY83 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 11J C 1201 |
| Chain | Residue |
| B | PRO169 |
| B | TRP172 |
| B | TRP173 |
| B | HIS216 |
| C | ILE30 |
| C | TRP35 |
| C | MET39 |
| C | SER42 |
| C | ARG46 |
| D | TYR91 |
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 | ARG55-GLY64 |
| site_id | PS01000 |
| Number of Residues | 25 |
| Details | SDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPLsphItiyrwsLpmamSicHRgT |
| Chain | Residue | Details |
| C | ARG24-THR48 |
| site_id | PS01001 |
| Number of Residues | 14 |
| Details | SDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtwnGIRHLiWDlG |
| Chain | Residue | Details |
| C | HIS101-GLY114 |
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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8K2B3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8K2B3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"UniProtKB","id":"P31040","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P31040","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8K2B3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 91 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| 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_FI11 |
| Number of Residues | 72 |
| Details | Region: {"description":"Interaction with SDHAF1","evidences":[{"source":"UniProtKB","id":"P21912","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZOY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQA3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 136 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 41 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 14 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZP0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
