6MYS
Avian mitochondrial complex II with Atpenin A5 bound, sidechain outside
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000104 | molecular_function | succinate dehydrogenase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005749 | cellular_component | mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) |
| 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 | 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 | 0005739 | cellular_component | mitochondrion |
| C | 0005749 | cellular_component | mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0006121 | biological_process | mitochondrial electron transport, succinate to ubiquinone |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016020 | cellular_component | membrane |
| C | 0045281 | cellular_component | succinate dehydrogenase complex |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005740 | cellular_component | mitochondrial envelope |
| D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | binding site for residue FAD A 1001 |
| Chain | Residue |
| A | GLY25 |
| A | SER55 |
| A | HIS56 |
| A | THR57 |
| A | ALA59 |
| A | ALA60 |
| A | GLN61 |
| A | GLY62 |
| A | GLY63 |
| A | TYR176 |
| A | PHE177 |
| A | ALA26 |
| A | ALA178 |
| A | ALA212 |
| A | THR213 |
| A | GLY214 |
| A | ASP232 |
| A | LEU263 |
| A | HIS364 |
| A | TYR365 |
| A | GLY396 |
| A | GLU397 |
| A | GLY27 |
| A | ARG408 |
| A | ALA411 |
| A | ASN412 |
| A | SER413 |
| A | LEU414 |
| A | LEU417 |
| A | OAA1003 |
| A | HOH1108 |
| A | GLY28 |
| A | ALA29 |
| A | VAL47 |
| A | THR48 |
| A | LYS49 |
| A | LEU50 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue K A 1002 |
| Chain | Residue |
| A | TYR365 |
| A | ASN366 |
| A | MET367 |
| A | GLY368 |
| A | GLU397 |
| A | ALA399 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue OAA A 1003 |
| Chain | Residue |
| A | GLY62 |
| A | PHE130 |
| A | HIS253 |
| A | LEU263 |
| A | THR265 |
| A | GLU266 |
| A | ARG297 |
| A | HIS364 |
| A | ARG408 |
| A | GLY410 |
| A | ALA411 |
| A | FAD1001 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue FES B 1001 |
| Chain | Residue |
| B | SER64 |
| B | CYS65 |
| B | ARG66 |
| B | GLY68 |
| B | CYS70 |
| B | GLY71 |
| B | CYS73 |
| B | CYS85 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue SF4 B 1002 |
| Chain | Residue |
| B | CYS158 |
| B | ILE159 |
| B | LEU160 |
| B | CYS161 |
| B | ALA162 |
| B | CYS163 |
| B | CYS164 |
| B | MET185 |
| B | CYS225 |
| B | PRO226 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue F3S B 1003 |
| Chain | Residue |
| B | CYS168 |
| B | TYR178 |
| B | CYS215 |
| B | HIS216 |
| B | THR217 |
| B | ILE218 |
| B | MET219 |
| B | ASN220 |
| B | CYS221 |
| B | ILE235 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue AT5 C 202 |
| Chain | Residue |
| B | PRO169 |
| B | SER170 |
| B | TRP173 |
| B | HIS216 |
| B | ILE218 |
| C | ILE27 |
| C | MET36 |
| C | SER39 |
| C | ILE40 |
| C | ARG43 |
| D | TYR58 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue HEM C 201 |
| Chain | Residue |
| C | SER50 |
| C | HIS98 |
| C | THR99 |
| C | HIS105 |
| D | ARG14 |
| D | LEU20 |
| D | LEU43 |
| D | HIS46 |
| D | GLY50 |
| B | HIS216 |
| C | HIS42 |
| C | ARG43 |
| C | GLY46 |
| C | LEU49 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue UMQ C 203 |
| Chain | Residue |
| B | ARG223 |
| C | TRP32 |
| C | SER33 |
| C | LEU34 |
| C | ALA37 |
| C | GLU120 |
| D | TYR88 |
| D | TYR89 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue 3PE D 201 |
| Chain | Residue |
| C | LEU95 |
| C | MET140 |
| D | ALA27 |
| D | TYR28 |
| D | VAL97 |
| D | ALA98 |
| D | TRP101 |
Functional Information from PROSITE/UniProt
| 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 |
| 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:16371358 |
| Chain | Residue | Details |
| B | CYS158 | |
| B | CYS161 | |
| B | CYS164 | |
| B | CYS168 | |
| B | CYS215 | |
| B | CYS221 | |
| B | CYS225 | |
| A | ARG297 | |
| D | VAL35-ILE55 | |
| D | ILE65-PHE86 | |
| B | CYS85 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256 |
| Chain | Residue | Details |
| A | SER413 | |
| A | THR48 | |
| A | GLY25 | |
| A | ASP232 | |
| A | GLU397 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256 |
| Chain | Residue | Details |
| A | ARG408 | |
| A | HIS253 | |
| A | THR265 | |
| A | HIS364 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Tele-8alpha-FAD histidine => ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256 |
| Chain | Residue | Details |
| A | HIS56 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256 |
| Chain | Residue | Details |
| D | TYR58 |
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 |
