6MYT
Avian mitochondrial complex II with Atpenin A5 bound, sidechain in pocket
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0005749 | cellular_component | obsolete 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 | 0045273 | cellular_component | respiratory chain complex II (succinate dehydrogenase) |
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 | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0009055 | molecular_function | electron transfer activity |
C | 0016020 | cellular_component | membrane |
C | 0045281 | cellular_component | obsolete 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 | 38 |
Details | binding site for residue FAD A 1001 |
Chain | Residue |
A | GLY25 |
A | HIS56 |
A | THR57 |
A | ALA59 |
A | ALA60 |
A | GLN61 |
A | GLY62 |
A | GLY63 |
A | TYR176 |
A | PHE177 |
A | ALA178 |
A | ALA26 |
A | ALA212 |
A | THR213 |
A | GLY214 |
A | ASP232 |
A | LEU263 |
A | HIS364 |
A | TYR365 |
A | GLY396 |
A | GLU397 |
A | ARG408 |
A | GLY27 |
A | ALA411 |
A | ASN412 |
A | SER413 |
A | LEU414 |
A | LEU417 |
A | OAA1002 |
A | HOH1113 |
A | HOH1123 |
A | HOH1166 |
A | GLY28 |
A | ALA29 |
A | THR48 |
A | LYS49 |
A | LEU50 |
A | SER55 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue OAA A 1002 |
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 | AC3 |
Number of Residues | 6 |
Details | binding site for residue K A 1003 |
Chain | Residue |
A | TYR365 |
A | ASN366 |
A | MET367 |
A | GLY368 |
A | GLU397 |
A | ALA399 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue PEG A 1005 |
Chain | Residue |
A | HIS227 |
A | ARG469 |
A | GLN473 |
A | GLU521 |
B | ARG63 |
site_id | AC5 |
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 | AC6 |
Number of Residues | 8 |
Details | binding site for residue SF4 B 1002 |
Chain | Residue |
B | CYS158 |
B | ILE159 |
B | LEU160 |
B | CYS161 |
B | ALA162 |
B | CYS164 |
B | MET185 |
B | CYS225 |
site_id | AC7 |
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 | AC8 |
Number of Residues | 14 |
Details | binding site for residue AT5 C 202 |
Chain | Residue |
D | ASP57 |
D | TYR58 |
B | PRO169 |
B | SER170 |
B | TRP172 |
B | TRP173 |
B | HIS216 |
B | ILE218 |
C | ILE27 |
C | TRP32 |
C | MET36 |
C | SER39 |
C | ILE40 |
C | ARG43 |
site_id | AC9 |
Number of Residues | 17 |
Details | binding site for residue HEM C 201 |
Chain | Residue |
B | HIS216 |
B | HOH1143 |
C | HIS42 |
C | ARG43 |
C | GLY46 |
C | LEU49 |
C | SER50 |
C | HIS98 |
C | THR99 |
C | GLY102 |
C | HIS105 |
D | ARG14 |
D | LEU20 |
D | LEU43 |
D | HIS46 |
D | GLY50 |
D | VAL54 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue UMQ C 203 |
Chain | Residue |
C | LYS31 |
C | TRP32 |
C | SER33 |
C | LEU34 |
C | THR41 |
C | PHE93 |
C | GLU120 |
D | TYR88 |
D | TYR89 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue 3PE D 201 |
Chain | Residue |
C | GLY52 |
C | LEU91 |
C | LEU95 |
C | MET140 |
D | ALA27 |
D | TYR28 |
D | VAL97 |
D | TRP101 |
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 | 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 |
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 |
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 |
A | ARG297 | |
B | CYS221 | |
B | CYS225 | |
D | VAL35-ILE55 | |
D | ILE65-PHE86 | |
B | CYS85 | |
B | CYS158 | |
B | CYS161 | |
B | CYS164 | |
B | CYS168 | |
B | CYS215 |
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 | GLY25 | |
A | THR48 | |
A | ASP232 | |
A | GLU397 | |
A | SER413 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256 |
Chain | Residue | Details |
A | HIS253 | |
A | THR265 | |
A | HIS364 | |
A | ARG408 |
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 |