2GMJ
Structure of Porcine Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004174 | molecular_function | electron-transferring-flavoprotein dehydrogenase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0022900 | biological_process | electron transport chain |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048039 | molecular_function | ubiquinone binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0004174 | molecular_function | electron-transferring-flavoprotein dehydrogenase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0022900 | biological_process | electron transport chain |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048039 | molecular_function | ubiquinone binding |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 610 |
| Chain | Residue |
| A | LEU504 |
| A | CYS528 |
| A | PRO529 |
| A | CYS553 |
| A | VAL554 |
| A | CYS556 |
| A | LYS557 |
| A | CYS559 |
| A | TRP570 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD A 611 |
| Chain | Residue |
| A | GLY42 |
| A | GLY44 |
| A | PRO45 |
| A | ALA46 |
| A | GLU71 |
| A | LYS72 |
| A | HIS79 |
| A | SER82 |
| A | GLY83 |
| A | ALA84 |
| A | CYS85 |
| A | ALA167 |
| A | ALA212 |
| A | GLU213 |
| A | GLY214 |
| A | HIS218 |
| A | PHE275 |
| A | LEU333 |
| A | GLY353 |
| A | CYS354 |
| A | ILE364 |
| A | LYS365 |
| A | GLY366 |
| A | THR367 |
| A | HOH706 |
| A | HOH719 |
| A | HOH801 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 612 |
| Chain | Residue |
| B | LEU504 |
| B | CYS528 |
| B | PRO529 |
| B | VAL532 |
| B | CYS553 |
| B | VAL554 |
| B | CYS556 |
| B | LYS557 |
| B | CYS559 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD B 613 |
| Chain | Residue |
| B | GLY42 |
| B | GLY44 |
| B | PRO45 |
| B | ALA46 |
| B | GLU71 |
| B | LYS72 |
| B | HIS79 |
| B | SER82 |
| B | GLY83 |
| B | ALA84 |
| B | CYS85 |
| B | ALA167 |
| B | GLU213 |
| B | GLY214 |
| B | HIS218 |
| B | PHE275 |
| B | TYR277 |
| B | ARG331 |
| B | LEU333 |
| B | GLY353 |
| B | CYS354 |
| B | ILE364 |
| B | LYS365 |
| B | GLY366 |
| B | THR367 |
| B | VAL572 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE TBU A 621 |
| Chain | Residue |
| A | ILE364 |
| A | HOH788 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TBU A 622 |
| Chain | Residue |
| A | TYR271 |
| A | THR438 |
| A | TBU623 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE TBU A 623 |
| Chain | Residue |
| A | LEU131 |
| A | TBU622 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE TBU A 624 |
| Chain | Residue |
| A | LYS324 |
| A | LEU491 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE TBU B 625 |
| Chain | Residue |
| B | TBU626 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE TBU B 626 |
| Chain | Residue |
| B | GLY273 |
| B | TBU625 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | Intramembrane: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17050691","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q921G7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q16134","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | THR80 | |
| A | CYS85 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | THR80 | |
| B | CYS85 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 281 |
| Chain | Residue | Details |
| A | SER82 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | ARG331 | activator, hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
| A | THR367 | electrostatic stabiliser |
| A | CYS528 | activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand |
| A | CYS553 | activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand |
| A | CYS556 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
| A | CYS559 | activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 281 |
| Chain | Residue | Details |
| B | SER82 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | ARG331 | activator, hydrogen bond acceptor, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay |
| B | THR367 | electrostatic stabiliser |
| B | CYS528 | activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand |
| B | CYS553 | activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand |
| B | CYS556 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
| B | CYS559 | activator, attractive charge-charge interaction, electrostatic stabiliser, metal ligand |
