1NEK
Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound
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 | 0045281 | cellular_component | obsolete succinate dehydrogenase complex |
A | 0045282 | cellular_component | obsolete plasma membrane succinate dehydrogenase complex |
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 | 0045281 | cellular_component | obsolete succinate dehydrogenase complex |
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 | 0045281 | cellular_component | obsolete succinate dehydrogenase complex |
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 | 0045281 | cellular_component | obsolete succinate dehydrogenase complex |
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 | GLY402 |
A | FAD601 |
A | HOH614 |
A | PHE126 |
A | HIS242 |
A | THR254 |
A | GLU255 |
A | ARG286 |
A | HIS354 |
A | ARG399 |
A | GLY401 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 590 |
Chain | Residue |
A | TYR355 |
A | MET356 |
A | MET357 |
A | GLY358 |
A | GLU388 |
A | ALA390 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA B 311 |
Chain | Residue |
B | ASP187 |
B | THR190 |
site_id | AC4 |
Number of Residues | 36 |
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 | 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 | THR213 |
A | ASN214 |
A | ASP221 |
A | LEU252 |
A | TYR355 |
A | GLY387 |
A | GLU388 |
A | ARG399 |
A | GLY402 |
A | ASN403 |
A | SER404 |
A | LEU405 |
A | LEU408 |
A | OAA589 |
A | HOH617 |
site_id | AC5 |
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 | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 B 303 |
Chain | Residue |
B | CYS149 |
B | ILE150 |
B | CYS152 |
B | ALA153 |
B | CYS155 |
B | ALA173 |
B | CYS216 |
B | LEU220 |
site_id | AC7 |
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 | AC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM C 305 |
Chain | Residue |
D | GLY75 |
D | MET76 |
D | GLN78 |
B | HIS207 |
C | HIS30 |
C | ARG31 |
C | GLY34 |
C | THR37 |
C | PHE38 |
C | HIS84 |
C | VAL85 |
C | GLY88 |
C | ILE89 |
C | CDN308 |
C | HOH311 |
D | ALA23 |
D | THR27 |
D | ILE68 |
D | HIS71 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE UQ2 D 306 |
Chain | Residue |
B | TRP164 |
B | ILE209 |
C | LEU15 |
C | PHE20 |
C | SER27 |
C | ILE28 |
D | TYR83 |
site_id | BC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE CDN C 308 |
Chain | Residue |
C | VAL41 |
C | LEU44 |
C | SER51 |
C | ALA61 |
C | SER62 |
C | LEU78 |
C | VAL115 |
C | LEU123 |
C | VAL126 |
C | LEU127 |
C | TRP129 |
C | HEM305 |
C | EPH309 |
D | ILE30 |
D | PHE37 |
D | GLY41 |
D | LEU43 |
D | TRP48 |
D | ILE68 |
D | HOH315 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EPH C 309 |
Chain | Residue |
C | LYS107 |
C | LYS111 |
C | TRP129 |
C | CDN308 |
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 | 23 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
D | MET1-ASP15 | |
B | CYS216 | |
D | THR81-ARG90 | |
B | CYS75 | |
B | CYS149 | |
B | CYS152 | |
B | CYS155 | |
B | CYS159 | |
B | CYS206 | |
B | CYS212 |
site_id | SWS_FT_FI2 |
Number of Residues | 65 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
D | PHE16-PHE36 | |
D | VAL59-LEU80 | |
D | LEU91-VAL115 | |
A | GLU388 | |
A | SER404 |
site_id | SWS_FT_FI3 |
Number of Residues | 21 |
Details | TOPO_DOM: Periplasmic => ECO:0000305 |
Chain | Residue | Details |
D | PHE37-LYS58 | |
A | THR254 | |
A | HIS354 | |
A | ARG399 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
D | HIS71 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12560550 |
Chain | Residue | Details |
D | TYR83 |
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 |