5XMJ
Crystal structure of quinol:fumarate reductase from Desulfovibrio gigas
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000104 | molecular_function | succinate dehydrogenase activity |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0009055 | molecular_function | electron transfer activity |
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 | 0022900 | biological_process | 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 | 0009060 | biological_process | aerobic respiration |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0022904 | biological_process | respiratory electron transport chain |
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 | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0016020 | cellular_component | membrane |
C | 0046872 | molecular_function | metal ion binding |
E | 0000104 | molecular_function | succinate dehydrogenase activity |
E | 0000166 | molecular_function | nucleotide binding |
E | 0005886 | cellular_component | plasma membrane |
E | 0009055 | molecular_function | electron transfer activity |
E | 0009061 | biological_process | anaerobic respiration |
E | 0016020 | cellular_component | membrane |
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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0006099 | biological_process | tricarboxylic acid cycle |
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 | 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 | 0006099 | biological_process | tricarboxylic acid cycle |
G | 0016020 | cellular_component | membrane |
G | 0046872 | molecular_function | metal ion binding |
I | 0000104 | molecular_function | succinate dehydrogenase activity |
I | 0000166 | molecular_function | nucleotide binding |
I | 0005886 | cellular_component | plasma membrane |
I | 0009055 | molecular_function | electron transfer activity |
I | 0009061 | biological_process | anaerobic respiration |
I | 0016020 | cellular_component | membrane |
I | 0016491 | molecular_function | oxidoreductase activity |
I | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
I | 0022900 | biological_process | electron transport chain |
I | 0050660 | molecular_function | flavin adenine dinucleotide binding |
J | 0006099 | biological_process | tricarboxylic acid cycle |
J | 0009055 | molecular_function | electron transfer activity |
J | 0009060 | biological_process | aerobic respiration |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0022904 | biological_process | respiratory electron transport chain |
J | 0046872 | molecular_function | metal ion binding |
J | 0051536 | molecular_function | iron-sulfur cluster binding |
J | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
J | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
J | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
K | 0006099 | biological_process | tricarboxylic acid cycle |
K | 0016020 | cellular_component | membrane |
K | 0046872 | molecular_function | metal ion binding |
M | 0000104 | molecular_function | succinate dehydrogenase activity |
M | 0000166 | molecular_function | nucleotide binding |
M | 0005886 | cellular_component | plasma membrane |
M | 0009055 | molecular_function | electron transfer activity |
M | 0009061 | biological_process | anaerobic respiration |
M | 0016020 | cellular_component | membrane |
M | 0016491 | molecular_function | oxidoreductase activity |
M | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
M | 0022900 | biological_process | electron transport chain |
M | 0050660 | molecular_function | flavin adenine dinucleotide binding |
N | 0006099 | biological_process | tricarboxylic acid cycle |
N | 0009055 | molecular_function | electron transfer activity |
N | 0009060 | biological_process | aerobic respiration |
N | 0016491 | molecular_function | oxidoreductase activity |
N | 0022904 | biological_process | respiratory electron transport chain |
N | 0046872 | molecular_function | metal ion binding |
N | 0051536 | molecular_function | iron-sulfur cluster binding |
N | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
N | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
N | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
O | 0006099 | biological_process | tricarboxylic acid cycle |
O | 0016020 | cellular_component | membrane |
O | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 31 |
Details | binding site for residue FAD A 701 |
Chain | Residue |
A | ILE11 |
A | HIS43 |
A | SER44 |
A | ALA46 |
A | ALA47 |
A | GLY49 |
A | GLY50 |
A | GLN180 |
A | ALA181 |
A | ALA215 |
A | THR216 |
A | GLY12 |
A | THR227 |
A | ASN228 |
A | GLY235 |
A | HIS369 |
A | GLY393 |
A | GLU394 |
A | ARG405 |
A | GLY408 |
A | SER410 |
A | LEU411 |
A | GLY13 |
A | ARG524 |
A | FUM702 |
A | ALA14 |
A | LEU15 |
A | ALA16 |
A | SER35 |
A | LEU36 |
A | SER42 |
site_id | AC2 |
Number of Residues | 14 |
Details | binding site for residue FUM A 702 |
Chain | Residue |
A | GLY49 |
A | PHE141 |
A | HIS257 |
A | LEU267 |
A | VAL268 |
A | THR269 |
A | GLU270 |
A | GLY271 |
A | ARG301 |
A | HIS369 |
A | ARG405 |
A | GLY407 |
A | GLY408 |
A | FAD701 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue F3S B 301 |
Chain | Residue |
B | CYS161 |
B | THR163 |
B | CYS208 |
B | MET209 |
B | GLY210 |
B | LEU211 |
B | LEU212 |
B | ALA213 |
B | CYS214 |
B | LEU228 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue SF4 B 302 |
Chain | Residue |
B | CYS151 |
B | GLU153 |
B | CYS154 |
B | CYS157 |
B | VAL174 |
B | CYS218 |
B | PRO219 |
B | ILE222 |
B | LEU224 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue FES B 303 |
Chain | Residue |
B | CYS57 |
B | GLY60 |
B | ILE61 |
B | CYS62 |
B | GLY63 |
B | CYS65 |
B | CYS77 |
site_id | AC6 |
Number of Residues | 16 |
Details | binding site for residue HEM C 301 |
Chain | Residue |
C | PHE34 |
C | HIS38 |
C | MET39 |
C | VAL42 |
C | VAL72 |
C | HIS129 |
C | MET130 |
C | VAL133 |
C | LEU134 |
C | ILE139 |
C | LYS143 |
C | ARG147 |
C | TYR156 |
C | LEU159 |
C | LEU160 |
C | GLY204 |
site_id | AC7 |
Number of Residues | 18 |
Details | binding site for residue HEM C 302 |
Chain | Residue |
C | TRP112 |
C | ALA119 |
C | LEU123 |
C | HIS166 |
C | VAL167 |
C | LYS177 |
C | GLN24 |
C | MET25 |
C | GLY28 |
C | LEU31 |
C | ILE32 |
C | LEU35 |
C | MET76 |
C | HIS79 |
C | PHE80 |
C | ALA83 |
C | LYS86 |
C | MET87 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue LMT C 303 |
Chain | Residue |
C | MET87 |
C | PRO88 |
C | PHE89 |
C | TRP94 |
C | LYS95 |
C | VAL116 |
C | ALA119 |
O | HIS9 |
O | ILE16 |
O | ILE81 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MQ7 C 304 |
Chain | Residue |
C | TRP36 |
C | ALA37 |
C | MET40 |
C | LEU41 |
C | ILE55 |
C | TYR63 |
site_id | AD1 |
Number of Residues | 11 |
Details | binding site for residue FUM E 702 |
Chain | Residue |
E | PHE141 |
E | HIS257 |
E | LEU267 |
E | VAL268 |
E | THR269 |
E | GLU270 |
E | ARG301 |
E | HIS369 |
E | ARG405 |
E | GLY407 |
E | GLY408 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue F3S F 301 |
Chain | Residue |
F | CYS161 |
F | THR163 |
F | CYS208 |
F | MET209 |
F | GLY210 |
F | LEU211 |
F | LEU212 |
F | ALA213 |
F | CYS214 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue SF4 F 302 |
Chain | Residue |
F | CYS151 |
F | CYS154 |
F | CYS157 |
F | VAL174 |
F | CYS218 |
F | ILE222 |
site_id | AD4 |
Number of Residues | 16 |
Details | binding site for residue HEM G 301 |
Chain | Residue |
G | PHE34 |
G | HIS38 |
G | MET39 |
G | VAL42 |
G | HIS129 |
G | ILE139 |
G | LYS143 |
G | SER144 |
G | ARG147 |
G | TYR156 |
G | LEU159 |
G | LEU160 |
G | GLY204 |
G | THR207 |
G | LEU208 |
G | PHE211 |
site_id | AD5 |
Number of Residues | 19 |
Details | binding site for residue HEM G 302 |
Chain | Residue |
F | MET209 |
G | GLN24 |
G | GLY28 |
G | LEU31 |
G | ILE32 |
G | HIS79 |
G | PHE80 |
G | ALA83 |
G | LYS86 |
G | MET87 |
G | TRP112 |
G | VAL116 |
G | ALA119 |
G | ILE122 |
G | LEU123 |
G | HIS166 |
G | VAL167 |
G | GLY170 |
G | LYS177 |
site_id | AD6 |
Number of Residues | 30 |
Details | binding site for residue FAD I 701 |
Chain | Residue |
I | GLY12 |
I | GLY13 |
I | ALA14 |
I | LEU15 |
I | ALA16 |
I | LEU36 |
I | SER42 |
I | HIS43 |
I | SER44 |
I | GLY49 |
I | GLY50 |
I | MET179 |
I | ALA181 |
I | ALA215 |
I | THR216 |
I | GLY217 |
I | THR227 |
I | ASN228 |
I | ILE231 |
I | GLY235 |
I | HIS369 |
I | GLY393 |
I | GLU394 |
I | ARG405 |
I | GLY408 |
I | SER410 |
I | LEU411 |
I | THR414 |
I | ARG524 |
I | FUM702 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for residue FUM I 702 |
Chain | Residue |
I | PHE141 |
I | HIS257 |
I | THR269 |
I | GLU270 |
I | ARG301 |
I | HIS369 |
I | ARG405 |
I | FAD701 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue SF4 J 302 |
Chain | Residue |
J | CYS151 |
J | CYS154 |
J | CYS157 |
J | VAL174 |
J | CYS218 |
J | ILE222 |
site_id | AD9 |
Number of Residues | 11 |
Details | binding site for residue HEM K 301 |
Chain | Residue |
K | PHE34 |
K | HIS38 |
K | VAL42 |
K | TYR63 |
K | HIS129 |
K | VAL133 |
K | SER144 |
K | ARG147 |
K | TYR156 |
K | LEU159 |
K | LEU208 |
site_id | AE1 |
Number of Residues | 16 |
Details | binding site for residue HEM K 302 |
Chain | Residue |
K | GLN24 |
K | MET25 |
K | GLY28 |
K | LEU31 |
K | ILE32 |
K | HIS79 |
K | ALA83 |
K | LYS86 |
K | TRP112 |
K | ALA119 |
K | LEU123 |
K | HIS166 |
K | VAL167 |
K | GLY170 |
K | ILE174 |
K | LYS177 |
site_id | AE2 |
Number of Residues | 33 |
Details | binding site for residue FAD M 701 |
Chain | Residue |
M | ILE11 |
M | GLY12 |
M | GLY13 |
M | ALA14 |
M | LEU15 |
M | ALA16 |
M | SER35 |
M | LEU36 |
M | SER42 |
M | HIS43 |
M | SER44 |
M | ALA47 |
M | GLN48 |
M | GLY49 |
M | GLY50 |
M | MET179 |
M | GLN180 |
M | ALA181 |
M | ALA215 |
M | THR216 |
M | GLY217 |
M | THR227 |
M | ASN228 |
M | GLY235 |
M | HIS369 |
M | TYR370 |
M | GLU394 |
M | GLY408 |
M | SER410 |
M | LEU411 |
M | THR414 |
M | ARG524 |
M | FUM702 |
site_id | AE3 |
Number of Residues | 9 |
Details | binding site for residue FUM M 702 |
Chain | Residue |
M | HIS257 |
M | LEU267 |
M | VAL268 |
M | THR269 |
M | GLU270 |
M | ARG301 |
M | HIS369 |
M | ARG405 |
M | FAD701 |
site_id | AE4 |
Number of Residues | 10 |
Details | binding site for residue F3S N 301 |
Chain | Residue |
N | CYS161 |
N | THR163 |
N | CYS208 |
N | MET209 |
N | GLY210 |
N | LEU211 |
N | LEU212 |
N | ALA213 |
N | CYS214 |
N | LEU228 |
site_id | AE5 |
Number of Residues | 5 |
Details | binding site for residue SF4 N 302 |
Chain | Residue |
N | CYS151 |
N | CYS154 |
N | CYS157 |
N | VAL174 |
N | CYS218 |
site_id | AE6 |
Number of Residues | 10 |
Details | binding site for residue LMT O 301 |
Chain | Residue |
C | HIS9 |
C | ILE16 |
C | ILE81 |
O | MET87 |
O | PRO88 |
O | PHE89 |
O | TRP94 |
O | LYS95 |
O | ARG98 |
O | VAL116 |
site_id | AE7 |
Number of Residues | 14 |
Details | binding site for residue HEM O 302 |
Chain | Residue |
O | PHE34 |
O | HIS38 |
O | MET39 |
O | HIS129 |
O | VAL133 |
O | ILE139 |
O | SER144 |
O | LEU148 |
O | TYR156 |
O | LEU159 |
O | LEU160 |
O | GLY204 |
O | THR207 |
O | PHE211 |
site_id | AE8 |
Number of Residues | 19 |
Details | binding site for residue HEM O 303 |
Chain | Residue |
O | GLN24 |
O | MET25 |
O | GLY28 |
O | LEU31 |
O | ILE32 |
O | HIS79 |
O | PHE80 |
O | ALA83 |
O | LYS86 |
O | MET87 |
O | TRP112 |
O | ALA119 |
O | ILE122 |
O | LEU123 |
O | HIS166 |
O | VAL167 |
O | GLY170 |
O | LYS177 |
O | TYR178 |
site_id | AE9 |
Number of Residues | 32 |
Details | binding site for Di-peptide FAD E 701 and HIS E 43 |
Chain | Residue |
E | ILE11 |
E | GLY12 |
E | GLY13 |
E | ALA14 |
E | LEU15 |
E | ALA16 |
E | SER35 |
E | LEU36 |
E | VAL37 |
E | SER42 |
E | SER44 |
E | SER45 |
E | ALA46 |
E | ALA47 |
E | GLY49 |
E | GLY50 |
E | MET179 |
E | ALA181 |
E | ALA215 |
E | THR216 |
E | GLY217 |
E | THR227 |
E | ASN228 |
E | ALA229 |
E | ILE231 |
E | GLU394 |
E | GLY408 |
E | ASN409 |
E | SER410 |
E | LEU411 |
E | THR414 |
E | ARG524 |
site_id | AF1 |
Number of Residues | 13 |
Details | binding site for Di-peptide FES F 303 and CYS F 65 |
Chain | Residue |
F | PHE55 |
F | CYS56 |
F | CYS57 |
F | ARG58 |
F | ILE61 |
F | CYS62 |
F | GLY63 |
F | SER64 |
F | ALA66 |
F | MET67 |
F | LEU75 |
F | ALA76 |
F | CYS77 |
site_id | AF2 |
Number of Residues | 8 |
Details | binding site for Di-peptide PRO I 608 and PHE I 612 |
Chain | Residue |
I | ASN605 |
I | GLU606 |
I | LEU607 |
I | PRO609 |
I | GLU610 |
I | LYS611 |
I | VAL613 |
I | ILE614 |
site_id | AF3 |
Number of Residues | 8 |
Details | binding site for Di-peptide PRO I 608 and PHE I 612 |
Chain | Residue |
I | ASN605 |
I | GLU606 |
I | LEU607 |
I | PRO609 |
I | GLU610 |
I | LYS611 |
I | VAL613 |
I | ILE614 |
site_id | AF4 |
Number of Residues | 8 |
Details | binding site for Di-peptide PRO I 608 and PHE I 612 |
Chain | Residue |
I | ASN605 |
I | GLU606 |
I | LEU607 |
I | PRO609 |
I | GLU610 |
I | LYS611 |
I | VAL613 |
I | ILE614 |
site_id | AF5 |
Number of Residues | 8 |
Details | binding site for Di-peptide PRO I 608 and PHE I 612 |
Chain | Residue |
I | ASN605 |
I | GLU606 |
I | LEU607 |
I | PRO609 |
I | GLU610 |
I | LYS611 |
I | VAL613 |
I | ILE614 |
site_id | AF6 |
Number of Residues | 13 |
Details | binding site for Di-peptide F3S J 301 and CYS J 214 |
Chain | Residue |
J | CYS161 |
J | THR163 |
J | CYS208 |
J | MET209 |
J | GLY210 |
J | LEU211 |
J | LEU212 |
J | ALA213 |
J | GLU215 |
J | ASP216 |
J | VAL217 |
J | CYS218 |
J | LEU224 |
site_id | AF7 |
Number of Residues | 14 |
Details | binding site for Di-peptide FES J 303 and CYS J 65 |
Chain | Residue |
J | ASP54 |
J | PHE55 |
J | CYS57 |
J | ARG58 |
J | GLY60 |
J | ILE61 |
J | CYS62 |
J | GLY63 |
J | SER64 |
J | ALA66 |
J | MET67 |
J | LEU75 |
J | ALA76 |
J | CYS77 |
site_id | AF8 |
Number of Residues | 12 |
Details | binding site for Di-peptide FES N 303 and CYS N 65 |
Chain | Residue |
N | PHE55 |
N | CYS57 |
N | ARG58 |
N | ILE61 |
N | CYS62 |
N | GLY63 |
N | SER64 |
N | ALA66 |
N | MET67 |
N | LEU75 |
N | ALA76 |
N | CYS77 |
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. CRAGICGSC |
Chain | Residue | Details |
B | CYS57-CYS65 |
site_id | PS00198 |
Number of Residues | 12 |
Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiECGcCVaACG |
Chain | Residue | Details |
B | CYS151-GLY162 |
site_id | PS00504 |
Number of Residues | 10 |
Details | FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHSsaAqGG |
Chain | Residue | Details |
A | ARG41-GLY50 |