2BS3
GLU C180 -> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000104 | molecular_function | succinate dehydrogenase activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
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 | 0005886 | cellular_component | plasma membrane |
B | 0006099 | biological_process | tricarboxylic acid cycle |
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 | 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 | 0005886 | cellular_component | plasma membrane |
C | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0016020 | cellular_component | membrane |
C | 0046872 | molecular_function | metal ion binding |
D | 0000104 | molecular_function | succinate dehydrogenase activity |
D | 0005886 | cellular_component | plasma membrane |
D | 0008177 | molecular_function | succinate dehydrogenase (quinone) activity |
D | 0009055 | molecular_function | electron transfer activity |
D | 0009061 | biological_process | anaerobic respiration |
D | 0016020 | cellular_component | membrane |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
D | 0022900 | biological_process | electron transport chain |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0005886 | cellular_component | plasma membrane |
E | 0006099 | biological_process | tricarboxylic acid cycle |
E | 0009055 | molecular_function | electron transfer activity |
E | 0009060 | biological_process | aerobic respiration |
E | 0016020 | cellular_component | membrane |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0022904 | biological_process | respiratory electron transport chain |
E | 0046872 | molecular_function | metal ion binding |
E | 0051536 | molecular_function | iron-sulfur cluster binding |
E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
E | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
F | 0005886 | cellular_component | plasma membrane |
F | 0006099 | biological_process | tricarboxylic acid cycle |
F | 0016020 | cellular_component | membrane |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A1658 |
Chain | Residue |
A | SER371 |
A | MET372 |
A | GLY373 |
A | GLU393 |
A | ALA395 |
A | HOH2156 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA D1658 |
Chain | Residue |
D | GLU393 |
D | ALA395 |
D | HOH2162 |
D | SER371 |
D | MET372 |
D | GLY373 |
site_id | AC3 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD A1656 |
Chain | Residue |
A | GLY12 |
A | GLY13 |
A | GLY14 |
A | LEU15 |
A | ALA16 |
A | SER35 |
A | LEU36 |
A | ILE37 |
A | SER42 |
A | HIS43 |
A | SER44 |
A | ALA47 |
A | GLY49 |
A | GLY50 |
A | LYS179 |
A | ALA181 |
A | ALA215 |
A | THR216 |
A | GLY217 |
A | THR227 |
A | ASN228 |
A | THR235 |
A | HIS369 |
A | TYR370 |
A | GLY392 |
A | GLU393 |
A | ARG404 |
A | GLY407 |
A | ASN408 |
A | SER409 |
A | VAL410 |
A | CIT1657 |
A | HOH2269 |
A | HOH2270 |
A | HOH2271 |
A | HOH2272 |
A | HOH2273 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CIT A1657 |
Chain | Residue |
A | ALA46 |
A | GLN48 |
A | GLY49 |
A | PHE141 |
A | GLN255 |
A | HIS257 |
A | LEU267 |
A | THR269 |
A | GLU270 |
A | ARG301 |
A | HIS369 |
A | ARG404 |
A | GLY406 |
A | FAD1656 |
A | HOH2274 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES B1240 |
Chain | Residue |
B | VAL56 |
B | CYS57 |
B | ARG58 |
B | GLY60 |
B | ILE61 |
B | CYS62 |
B | GLY63 |
B | CYS65 |
B | CYS77 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE F3S B1241 |
Chain | Residue |
B | CYS161 |
B | THR163 |
B | CYS208 |
B | MET209 |
B | THR210 |
B | LEU211 |
B | LEU212 |
B | ALA213 |
B | CYS214 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 B1242 |
Chain | Residue |
B | CYS151 |
B | ILE152 |
B | GLU153 |
B | CYS154 |
B | GLY155 |
B | CYS157 |
B | CYS218 |
B | PRO219 |
B | LYS220 |
site_id | AC8 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEM C1255 |
Chain | Residue |
C | ALA97 |
C | LYS100 |
C | PHE101 |
C | TRP126 |
C | GLY133 |
C | MET136 |
C | PHE137 |
C | HIS182 |
C | GLY186 |
C | LEU190 |
C | LYS193 |
C | HEM1256 |
C | HOH2046 |
C | HOH2047 |
B | HOH2142 |
C | GLN30 |
C | SER31 |
C | GLY34 |
C | LEU37 |
C | PHE90 |
C | HIS93 |
C | ALA94 |
site_id | AC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HEM C1256 |
Chain | Residue |
C | PHE40 |
C | MET41 |
C | HIS44 |
C | LEU82 |
C | ALA83 |
C | HIS143 |
C | MET147 |
C | ILE154 |
C | SER159 |
C | ARG162 |
C | TYR172 |
C | LEU176 |
C | GLY224 |
C | PHE228 |
C | HEM1255 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE LMT C1257 |
Chain | Residue |
C | PHE101 |
C | PRO102 |
C | ASN104 |
C | TYR108 |
C | MET131 |
F | PHE95 |
F | MET98 |
F | ARG99 |
site_id | BC2 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE FAD D1656 |
Chain | Residue |
D | GLY12 |
D | GLY13 |
D | GLY14 |
D | LEU15 |
D | ALA16 |
D | SER35 |
D | LEU36 |
D | ILE37 |
D | SER42 |
D | HIS43 |
D | SER44 |
D | ALA47 |
D | GLY49 |
D | GLY50 |
D | LYS179 |
D | GLU180 |
D | ALA181 |
D | ALA215 |
D | THR216 |
D | GLY217 |
D | THR227 |
D | ASN228 |
D | THR235 |
D | HIS369 |
D | TYR370 |
D | GLY392 |
D | GLU393 |
D | ARG404 |
D | GLY407 |
D | ASN408 |
D | SER409 |
D | VAL410 |
D | CIT1657 |
D | HOH2128 |
D | HOH2285 |
D | HOH2286 |
D | HOH2287 |
D | HOH2288 |
site_id | BC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CIT D1657 |
Chain | Residue |
D | ALA46 |
D | GLN48 |
D | GLY49 |
D | PHE141 |
D | GLN255 |
D | HIS257 |
D | LEU267 |
D | THR269 |
D | GLU270 |
D | ARG301 |
D | HIS369 |
D | ARG404 |
D | FAD1656 |
D | HOH2289 |
D | HOH2291 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES E1240 |
Chain | Residue |
E | VAL56 |
E | CYS57 |
E | ARG58 |
E | GLY60 |
E | ILE61 |
E | CYS62 |
E | GLY63 |
E | CYS65 |
E | CYS77 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE F3S E1241 |
Chain | Residue |
E | CYS161 |
E | THR163 |
E | CYS208 |
E | MET209 |
E | THR210 |
E | LEU211 |
E | LEU212 |
E | ALA213 |
E | CYS214 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 E1242 |
Chain | Residue |
E | CYS151 |
E | ILE152 |
E | GLU153 |
E | CYS154 |
E | GLY155 |
E | CYS157 |
E | CYS218 |
E | PRO219 |
E | LYS220 |
site_id | BC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM F1255 |
Chain | Residue |
F | GLN30 |
F | SER31 |
F | GLY34 |
F | LEU37 |
F | PHE90 |
F | HIS93 |
F | ALA94 |
F | ALA97 |
F | LYS100 |
F | PHE101 |
F | TRP126 |
F | GLY133 |
F | MET136 |
F | PHE137 |
F | VAL179 |
F | HIS182 |
F | GLY186 |
F | LEU190 |
F | LYS193 |
F | HEM1256 |
F | HOH2057 |
F | HOH2058 |
F | HOH2059 |
site_id | BC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HEM F1256 |
Chain | Residue |
F | PHE40 |
F | MET41 |
F | HIS44 |
F | LEU82 |
F | ALA83 |
F | HIS143 |
F | MET147 |
F | ILE154 |
F | SER159 |
F | ARG162 |
F | TYR172 |
F | LEU176 |
F | GLY224 |
F | PHE228 |
F | HEM1255 |
site_id | BC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LMT F1257 |
Chain | Residue |
C | LEU26 |
C | PHE95 |
C | MET98 |
C | ARG99 |
F | PHE101 |
F | PRO102 |
F | ASN104 |
F | TYR108 |
F | MET131 |
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. CiECGcCIaACG |
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. RSHSaaAqGG |
Chain | Residue | Details |
A | ARG41-GLY50 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P00363","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 38 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11248702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS4","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS4","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11248702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 180 |
Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 58 |
Details | Domain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 58 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 222 |
Details | Transmembrane: {"description":"Helical"} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 76 |
Details | Topological domain: {"description":"Periplasmic"} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 84 |
Details | Topological domain: {"description":"Cytoplasmic"} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11248702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS4","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1d4c |
Chain | Residue | Details |
A | HIS257 | |
A | ARG404 | |
A | HIS369 | |
A | ARG301 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1d4c |
Chain | Residue | Details |
D | HIS257 | |
D | ARG404 | |
D | HIS369 | |
D | ARG301 |