4YSY
Crystal structure of Mitochondrial rhodoquinol-fumarate reductase from Ascaris suum with N-[(2,4-dichlorophenyl)methyl]-2-(trifluoromethyl)benzamide
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005515 | molecular_function | protein binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0006099 | biological_process | tricarboxylic acid cycle |
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 | 0031966 | cellular_component | mitochondrial membrane |
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 | 0005739 | cellular_component | mitochondrion |
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 | 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 | 0005515 | molecular_function | protein binding |
C | 0005739 | cellular_component | mitochondrion |
C | 0005743 | cellular_component | mitochondrial inner 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 | 0020037 | molecular_function | heme binding |
C | 0031966 | cellular_component | mitochondrial membrane |
C | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
C | 0046872 | molecular_function | metal ion binding |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005740 | cellular_component | mitochondrial envelope |
D | 0005743 | cellular_component | mitochondrial inner membrane |
D | 0006099 | biological_process | tricarboxylic acid cycle |
D | 0006121 | biological_process | mitochondrial electron transport, succinate to ubiquinone |
D | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
D | 0016020 | cellular_component | membrane |
D | 0020037 | molecular_function | heme binding |
D | 0031966 | cellular_component | mitochondrial membrane |
D | 0043231 | cellular_component | intracellular membrane-bounded organelle |
D | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
D | 0046872 | molecular_function | metal ion binding |
D | 0048039 | molecular_function | ubiquinone binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0005515 | molecular_function | protein binding |
E | 0005739 | cellular_component | mitochondrion |
E | 0005743 | cellular_component | mitochondrial inner membrane |
E | 0006099 | biological_process | tricarboxylic acid cycle |
E | 0006121 | biological_process | mitochondrial electron transport, succinate to ubiquinone |
E | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
E | 0009055 | molecular_function | electron transfer activity |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
E | 0022900 | biological_process | electron transport chain |
E | 0031966 | cellular_component | mitochondrial membrane |
E | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0005515 | molecular_function | protein binding |
F | 0005739 | cellular_component | mitochondrion |
F | 0005743 | cellular_component | mitochondrial inner membrane |
F | 0006099 | biological_process | tricarboxylic acid cycle |
F | 0006121 | biological_process | mitochondrial electron transport, succinate to ubiquinone |
F | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
F | 0009055 | molecular_function | electron transfer activity |
F | 0009060 | biological_process | aerobic respiration |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0022904 | biological_process | respiratory electron transport chain |
F | 0031966 | cellular_component | mitochondrial membrane |
F | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
F | 0046872 | molecular_function | metal ion binding |
F | 0051536 | molecular_function | iron-sulfur cluster binding |
F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
F | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
G | 0005515 | molecular_function | protein binding |
G | 0005739 | cellular_component | mitochondrion |
G | 0005743 | cellular_component | mitochondrial inner membrane |
G | 0006099 | biological_process | tricarboxylic acid cycle |
G | 0006121 | biological_process | mitochondrial electron transport, succinate to ubiquinone |
G | 0009055 | molecular_function | electron transfer activity |
G | 0016020 | cellular_component | membrane |
G | 0020037 | molecular_function | heme binding |
G | 0031966 | cellular_component | mitochondrial membrane |
G | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
G | 0046872 | molecular_function | metal ion binding |
H | 0005515 | molecular_function | protein binding |
H | 0005737 | cellular_component | cytoplasm |
H | 0005739 | cellular_component | mitochondrion |
H | 0005740 | cellular_component | mitochondrial envelope |
H | 0005743 | cellular_component | mitochondrial inner membrane |
H | 0006099 | biological_process | tricarboxylic acid cycle |
H | 0006121 | biological_process | mitochondrial electron transport, succinate to ubiquinone |
H | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
H | 0016020 | cellular_component | membrane |
H | 0020037 | molecular_function | heme binding |
H | 0031966 | cellular_component | mitochondrial membrane |
H | 0043231 | cellular_component | intracellular membrane-bounded organelle |
H | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
H | 0046872 | molecular_function | metal ion binding |
H | 0048039 | molecular_function | ubiquinone binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue MLI A 701 |
Chain | Residue |
A | GLY85 |
A | FAD702 |
A | PHE153 |
A | HIS276 |
A | LEU286 |
A | THR288 |
A | GLU289 |
A | ARG320 |
A | HIS387 |
A | ARG432 |
site_id | AC2 |
Number of Residues | 35 |
Details | binding site for residue FAD A 702 |
Chain | Residue |
A | GLY48 |
A | ALA49 |
A | GLY50 |
A | GLY51 |
A | ALA52 |
A | VAL70 |
A | THR71 |
A | LYS72 |
A | MET73 |
A | SER78 |
A | HIS79 |
A | THR80 |
A | ALA82 |
A | ALA83 |
A | GLN84 |
A | GLY85 |
A | GLY86 |
A | TYR199 |
A | ALA201 |
A | ALA235 |
A | THR236 |
A | GLY237 |
A | THR247 |
A | ASP255 |
A | LEU286 |
A | HIS387 |
A | TYR388 |
A | GLY420 |
A | GLU421 |
A | ARG432 |
A | ALA435 |
A | SER437 |
A | LEU438 |
A | MLI701 |
A | HOH801 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue FES B 301 |
Chain | Residue |
B | SER88 |
B | CYS89 |
B | CYS94 |
B | GLY95 |
B | CYS97 |
B | CYS109 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SF4 B 302 |
Chain | Residue |
B | CYS182 |
B | CYS185 |
B | CYS188 |
B | CYS249 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue F3S B 303 |
Chain | Residue |
B | CYS192 |
B | TYR202 |
B | CYS239 |
B | HIS240 |
B | MET243 |
B | ASN244 |
B | CYS245 |
B | ALA256 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue E24 B 304 |
Chain | Residue |
B | PRO193 |
B | SER194 |
B | TRP197 |
B | HIS240 |
C | TRP69 |
C | SER72 |
C | GLY73 |
C | ARG76 |
D | ASP106 |
D | TYR107 |
site_id | AC7 |
Number of Residues | 16 |
Details | binding site for residue HEM C 201 |
Chain | Residue |
B | HIS240 |
C | HIS75 |
C | ARG76 |
C | GLY79 |
C | CYS80 |
C | MET82 |
C | ALA83 |
C | HIS131 |
C | THR132 |
D | ARG63 |
D | ALA66 |
D | MET69 |
D | ILE73 |
D | HIS95 |
D | VAL96 |
D | GLY99 |
site_id | AC8 |
Number of Residues | 11 |
Details | binding site for residue EPH D 201 |
Chain | Residue |
D | TRP154 |
C | THR85 |
C | VAL170 |
D | VAL70 |
D | ILE73 |
D | ALA76 |
D | TYR77 |
D | PHE78 |
D | HIS80 |
D | PHE150 |
D | GLU151 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue MLI E 701 |
Chain | Residue |
E | GLN84 |
E | GLY85 |
E | PHE153 |
E | HIS276 |
E | LEU286 |
E | THR288 |
E | GLU289 |
E | ARG320 |
E | HIS387 |
E | ARG432 |
E | ALA435 |
E | FAD702 |
site_id | AD1 |
Number of Residues | 35 |
Details | binding site for residue FAD E 702 |
Chain | Residue |
E | GLY48 |
E | ALA49 |
E | GLY50 |
E | GLY51 |
E | ALA52 |
E | THR71 |
E | LYS72 |
E | MET73 |
E | SER78 |
E | HIS79 |
E | THR80 |
E | ALA82 |
E | ALA83 |
E | GLN84 |
E | GLY85 |
E | GLY86 |
E | TYR199 |
E | ALA201 |
E | ALA235 |
E | THR236 |
E | GLY237 |
E | THR247 |
E | ASP255 |
E | LEU286 |
E | HIS387 |
E | TYR388 |
E | GLY420 |
E | GLU421 |
E | ARG432 |
E | ALA435 |
E | ASN436 |
E | SER437 |
E | LEU438 |
E | MLI701 |
E | HOH805 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue FES F 301 |
Chain | Residue |
F | SER88 |
F | CYS89 |
F | GLY92 |
F | CYS94 |
F | GLY95 |
F | CYS97 |
F | CYS109 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue SF4 F 302 |
Chain | Residue |
F | CYS182 |
F | CYS185 |
F | ALA186 |
F | CYS188 |
F | CYS249 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue F3S F 303 |
Chain | Residue |
F | CYS192 |
F | TYR202 |
F | CYS239 |
F | HIS240 |
F | THR241 |
F | MET243 |
F | ASN244 |
F | CYS245 |
site_id | AD5 |
Number of Residues | 10 |
Details | binding site for residue E24 F 304 |
Chain | Residue |
F | PRO193 |
F | SER194 |
F | TRP197 |
F | HIS240 |
G | TRP69 |
G | SER72 |
G | GLY73 |
G | ARG76 |
H | ASP106 |
H | TYR107 |
site_id | AD6 |
Number of Residues | 15 |
Details | binding site for residue HEM G 201 |
Chain | Residue |
F | HIS240 |
G | HIS75 |
G | ARG76 |
G | GLY79 |
G | CYS80 |
G | MET82 |
G | ALA83 |
G | HIS131 |
G | THR132 |
H | ARG63 |
H | ALA66 |
H | ILE73 |
H | HIS95 |
H | VAL96 |
H | GLY99 |
site_id | AD7 |
Number of Residues | 10 |
Details | binding site for residue EPH H 201 |
Chain | Residue |
G | THR85 |
G | VAL170 |
H | VAL70 |
H | ILE73 |
H | ALA76 |
H | TYR77 |
H | HIS80 |
H | PHE150 |
H | GLU151 |
H | TRP154 |
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 | CYS89-CYS97 |
site_id | PS00198 |
Number of Residues | 12 |
Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCSaSCP |
Chain | Residue | Details |
B | CYS182-PRO193 |
site_id | PS00504 |
Number of Residues | 10 |
Details | FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTtaAqGG |
Chain | Residue | Details |
A | ARG77-GLY86 |
site_id | PS01000 |
Number of Residues | 25 |
Details | SDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPIaphLtiykpqMtwmvSglHRvT |
Chain | Residue | Details |
C | ARG54-THR78 |
site_id | PS01001 |
Number of Residues | 14 |
Details | SDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtlnGIRFIgFDmA |
Chain | Residue | Details |
C | HIS131-ALA144 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PIRSR:PIRSR611281-1 |
Chain | Residue | Details |
A | ARG320 | |
B | CYS245 | |
B | CYS249 | |
F | CYS89 | |
F | CYS94 | |
F | CYS97 | |
F | CYS109 | |
F | CYS182 | |
F | CYS185 | |
F | CYS188 | |
F | CYS192 | |
E | ARG320 | |
F | CYS239 | |
F | CYS245 | |
F | CYS249 | |
H | GLY26-PHE59 | |
H | ASN105-ALA119 | |
B | CYS182 | |
B | CYS185 | |
B | CYS188 | |
B | CYS192 | |
B | CYS239 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VR9, ECO:0007744|PDB:3VRA, ECO:0007744|PDB:3VRB, ECO:0007744|PDB:4YSX, ECO:0007744|PDB:4YSY, ECO:0007744|PDB:4YSZ, ECO:0007744|PDB:4YT0, ECO:0007744|PDB:4YTM, ECO:0007744|PDB:4YTN, ECO:0007744|PDB:5C2T, ECO:0007744|PDB:5C3J |
Chain | Residue | Details |
A | ALA49 | |
E | THR71 | |
E | SER78 | |
E | THR80 | |
E | GLY86 | |
E | ALA201 | |
E | SER437 | |
E | LEU438 | |
A | THR71 | |
A | SER78 | |
A | THR80 | |
A | GLY86 | |
A | ALA201 | |
A | SER437 | |
A | LEU438 | |
E | ALA49 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VRA, ECO:0007744|PDB:4YSX, ECO:0007744|PDB:4YSY, ECO:0007744|PDB:4YSZ, ECO:0007744|PDB:4YT0, ECO:0007744|PDB:4YTM, ECO:0007744|PDB:4YTN, ECO:0007744|PDB:5C2T, ECO:0007744|PDB:5C3J |
Chain | Residue | Details |
A | ALA52 | |
E | ALA52 | |
H | ILE79-GLU83 | |
H | HIS142-LEU156 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VR9, ECO:0007744|PDB:3VRB, ECO:0007744|PDB:4YSX, ECO:0007744|PDB:4YSY, ECO:0007744|PDB:4YT0 |
Chain | Residue | Details |
A | LYS72 | |
E | LYS72 | |
G | SER72 | |
G | ARG76 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VR9, ECO:0007744|PDB:3VRA, ECO:0007744|PDB:3VRB, ECO:0007744|PDB:4YSX, ECO:0007744|PDB:4YSY, ECO:0007744|PDB:4YSZ, ECO:0007744|PDB:4YT0, ECO:0007744|PDB:4YTN, ECO:0007744|PDB:5C2T |
Chain | Residue | Details |
A | GLN84 | |
E | GLN84 |
site_id | SWS_FT_FI6 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VRB |
Chain | Residue | Details |
A | GLY85 | |
E | ARG432 | |
A | HIS276 | |
A | THR288 | |
A | GLU289 | |
A | ARG432 | |
E | GLY85 | |
E | HIS276 | |
E | THR288 | |
E | GLU289 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:4YSX, ECO:0007744|PDB:4YSY, ECO:0007744|PDB:4YSZ, ECO:0007744|PDB:4YT0, ECO:0007744|PDB:4YTM, ECO:0007744|PDB:5C2T, ECO:0007744|PDB:5C3J |
Chain | Residue | Details |
A | ASP255 | |
E | ASP255 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0007744|PDB:3VRB |
Chain | Residue | Details |
A | HIS387 | |
A | ALA435 | |
E | HIS387 | |
E | ALA435 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VR9, ECO:0007744|PDB:3VRA, ECO:0007744|PDB:3VRB, ECO:0007744|PDB:4YSX, ECO:0007744|PDB:4YSY, ECO:0007744|PDB:4YSZ, ECO:0007744|PDB:4YT0, ECO:0007744|PDB:4YTN, ECO:0007744|PDB:5C2T, ECO:0007744|PDB:5C3J |
Chain | Residue | Details |
A | GLU421 | |
E | GLU421 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Tele-8alpha-FAD histidine => ECO:0000255|PIRSR:PIRSR611281-4, ECO:0000269|PubMed:22577165, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VR9, ECO:0007744|PDB:3VRA, ECO:0007744|PDB:3VRB |
Chain | Residue | Details |
A | HIS79 | |
E | HIS79 |