5Z62
Structure of human cytochrome c oxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001666 | biological_process | response to hypoxia |
| A | 0004129 | molecular_function | cytochrome-c oxidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0006119 | biological_process | oxidative phosphorylation |
| A | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0009060 | biological_process | aerobic respiration |
| A | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| A | 0021549 | biological_process | cerebellum development |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0031966 | cellular_component | mitochondrial membrane |
| A | 0045277 | cellular_component | respiratory chain complex IV |
| A | 0045333 | biological_process | cellular respiration |
| A | 0046688 | biological_process | response to copper ion |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051602 | biological_process | response to electrical stimulus |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0001666 | biological_process | response to hypoxia |
| B | 0004129 | molecular_function | cytochrome-c oxidase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| B | 0007595 | biological_process | lactation |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0017004 | biological_process | cytochrome complex assembly |
| B | 0022900 | biological_process | electron transport chain |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0031966 | cellular_component | mitochondrial membrane |
| B | 0042773 | biological_process | ATP synthesis coupled electron transport |
| B | 0045277 | cellular_component | respiratory chain complex IV |
| B | 0045333 | biological_process | cellular respiration |
| B | 0045471 | biological_process | response to ethanol |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1902600 | biological_process | proton transmembrane transport |
| C | 0004129 | molecular_function | cytochrome-c oxidase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005743 | cellular_component | mitochondrial inner membrane |
| C | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| C | 0008535 | biological_process | respiratory chain complex IV assembly |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016020 | cellular_component | membrane |
| C | 0019646 | biological_process | aerobic electron transport chain |
| C | 0022904 | biological_process | respiratory electron transport chain |
| C | 0031966 | cellular_component | mitochondrial membrane |
| C | 0045277 | cellular_component | respiratory chain complex IV |
| C | 0045333 | biological_process | cellular respiration |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| D | 0045277 | cellular_component | respiratory chain complex IV |
| E | 0005743 | cellular_component | mitochondrial inner membrane |
| E | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| E | 0045277 | cellular_component | respiratory chain complex IV |
| F | 0005740 | cellular_component | mitochondrial envelope |
| F | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| F | 0045277 | cellular_component | respiratory chain complex IV |
| G | 0005743 | cellular_component | mitochondrial inner membrane |
| H | 0004129 | molecular_function | cytochrome-c oxidase activity |
| H | 0005739 | cellular_component | mitochondrion |
| H | 0005743 | cellular_component | mitochondrial inner membrane |
| H | 0006119 | biological_process | oxidative phosphorylation |
| H | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| H | 0016020 | cellular_component | membrane |
| H | 0021762 | biological_process | substantia nigra development |
| H | 0031966 | cellular_component | mitochondrial membrane |
| H | 0045277 | cellular_component | respiratory chain complex IV |
| H | 0045333 | biological_process | cellular respiration |
| H | 1902600 | biological_process | proton transmembrane transport |
| I | 0005515 | molecular_function | protein binding |
| I | 0005739 | cellular_component | mitochondrion |
| I | 0005743 | cellular_component | mitochondrial inner membrane |
| I | 0005758 | cellular_component | mitochondrial intermembrane space |
| I | 0006091 | biological_process | generation of precursor metabolites and energy |
| I | 0006119 | biological_process | oxidative phosphorylation |
| I | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| I | 0016020 | cellular_component | membrane |
| I | 0031966 | cellular_component | mitochondrial membrane |
| I | 0045277 | cellular_component | respiratory chain complex IV |
| I | 0045333 | biological_process | cellular respiration |
| J | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| J | 0045277 | cellular_component | respiratory chain complex IV |
| K | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| L | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| L | 0045277 | cellular_component | respiratory chain complex IV |
| M | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| M | 0045277 | cellular_component | respiratory chain complex IV |
| N | 0005515 | molecular_function | protein binding |
| N | 0005739 | cellular_component | mitochondrion |
| N | 0005743 | cellular_component | mitochondrial inner membrane |
| N | 0006120 | biological_process | mitochondrial electron transport, NADH to ubiquinone |
| N | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| N | 0008137 | molecular_function | NADH dehydrogenase (ubiquinone) activity |
| N | 0022904 | biological_process | respiratory electron transport chain |
| N | 0031966 | cellular_component | mitochondrial membrane |
| N | 0044877 | molecular_function | protein-containing complex binding |
| N | 0045271 | cellular_component | respiratory chain complex I |
| N | 0045277 | cellular_component | respiratory chain complex IV |
| N | 0045333 | biological_process | cellular respiration |
| N | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CU A 601 |
| Chain | Residue |
| A | HIS240 |
| A | HIS290 |
| A | HIS291 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 602 |
| Chain | Residue |
| A | HIS368 |
| A | ASP369 |
| B | GLU198 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue HEA A 603 |
| Chain | Residue |
| A | TYR54 |
| A | VAL58 |
| A | HIS61 |
| A | MET65 |
| A | MET69 |
| A | TRP126 |
| A | TYR371 |
| A | PHE377 |
| A | HIS378 |
| A | LEU381 |
| A | SER382 |
| A | VAL386 |
| A | MET390 |
| A | GLN428 |
| A | ARG438 |
| A | ARG439 |
| A | SER461 |
| A | MET468 |
| A | GLY27 |
| A | THR31 |
| A | ARG38 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue HEA A 604 |
| Chain | Residue |
| A | TRP126 |
| A | TRP236 |
| A | VAL243 |
| A | TYR244 |
| A | HIS290 |
| A | HIS291 |
| A | ILE312 |
| A | ALA313 |
| A | GLY317 |
| A | PHE348 |
| A | GLY352 |
| A | GLY355 |
| A | LEU358 |
| A | ALA359 |
| A | ASP364 |
| A | HIS368 |
| A | HIS376 |
| A | PHE377 |
| A | VAL380 |
| A | LEU381 |
| A | ARG438 |
| B | PRO69 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue PEE A 605 |
| Chain | Residue |
| A | PHE94 |
| A | PRO95 |
| A | ARG96 |
| A | MET97 |
| A | LEU159 |
| C | HIS9 |
| C | TRP57 |
| C | TRP58 |
| C | GLY82 |
| C | PHE86 |
| C | PEE301 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CU B 301 |
| Chain | Residue |
| B | HIS161 |
| B | CYS196 |
| B | GLU198 |
| B | CYS200 |
| B | MET207 |
| B | CU302 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CU B 302 |
| Chain | Residue |
| B | HIS161 |
| B | CYS196 |
| B | CYS200 |
| B | HIS204 |
| B | MET207 |
| B | CU301 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for residue PEE C 301 |
| Chain | Residue |
| A | PEE605 |
| C | TRP58 |
| C | THR62 |
| C | SER65 |
| C | THR66 |
| C | HIS71 |
| C | PHE86 |
| C | GLU90 |
| C | PHE93 |
| C | HIS207 |
| C | THR213 |
| C | PHE214 |
| C | ILE217 |
| C | ARG221 |
| C | HIS226 |
| C | HIS231 |
| C | HIS232 |
| C | PHE233 |
| C | GLY234 |
| C | PEE302 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue PEE C 302 |
| Chain | Residue |
| C | PHE203 |
| C | PEE301 |
| G | TRP86 |
| G | THR92 |
| G | LEU93 |
| G | PHE94 |
| G | ASN100 |
| C | TYR181 |
| C | SER184 |
| C | PHE186 |
| C | THR187 |
| C | ILE188 |
| C | PHE198 |
| C | GLY202 |
| site_id | AD1 |
| Number of Residues | 14 |
| Details | binding site for residue CDL C 303 |
| Chain | Residue |
| A | TRP288 |
| A | ASP298 |
| A | THR301 |
| A | PHE305 |
| C | PHE92 |
| C | PHE98 |
| C | TRP99 |
| C | TYR102 |
| C | HIS103 |
| C | ALA107 |
| N | LEU36 |
| N | ALA37 |
| N | ASN40 |
| N | ASP42 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN F 201 |
| Chain | Residue |
| F | CYS91 |
| F | CYS93 |
| F | CYS113 |
| F | CYS116 |
| F | ALA118 |
Functional Information from PROSITE/UniProt
| site_id | PS00078 |
| Number of Residues | 49 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavptlglktdaipgrlnqttftatrpgvyygq......CseiCganHsfM |
| Chain | Residue | Details |
| B | VAL159-MET207 |
| site_id | PS00077 |
| Number of Residues | 56 |
| Details | COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH |
| Chain | Residue | Details |
| A | TRP236-HIS291 |
| site_id | PS00848 |
| Number of Residues | 23 |
| Details | COX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VVWfwlhkgeaqrCprCGahYKL |
| Chain | Residue | Details |
| F | VAL100-LEU122 |
| site_id | PS01329 |
| Number of Residues | 18 |
| Details | COX6A Cytochrome c oxidase subunit VIa signature. IRtKpFpWGDGnHTlFhN |
| Chain | Residue | Details |
| G | ILE79-ASN96 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 135 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"30030519","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=I","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 378 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"30030519","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 35 |
| Details | Transmembrane: {"description":"Helical; Name=II","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=III","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 29 |
| Details | Transmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 29 |
| Details | Transmembrane: {"description":"Helical; Name=V","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 33 |
| Details | Transmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | Transmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=VIII","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=IX","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 29 |
| Details | Transmembrane: {"description":"Helical; Name=X","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical; Name=XI","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 31 |
| Details | Transmembrane: {"description":"Helical; Name=XII","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00401","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"30030519","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30030519","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 30 |
| Details | Transmembrane: {"description":"Helical; Name=I","evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 27 |
| Details | Transmembrane: {"description":"Helical; Name=II","evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=I","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=II","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 32 |
| Details | Transmembrane: {"description":"Helical; Name=III","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 27 |
| Details | Transmembrane: {"description":"Helical; Name=V","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 32 |
| Details | Transmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P00423","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI30 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI31 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI32 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10888","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI33 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19783","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI34 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P12787","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI35 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI36 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00428","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI37 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19536","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI38 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P07471","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI39 |
| Number of Residues | 46 |
| Details | Domain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI40 |
| Number of Residues | 10 |
| Details | Motif: {"description":"Cx9C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI41 |
| Number of Residues | 11 |
| Details | Motif: {"description":"Cx10C motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI42 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P04038","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI43 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P07470","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI44 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P48771","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI45 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P13183","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI46 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P00430","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI47 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17665","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI48 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P10175","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI49 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30030519","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI50 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q62425","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI51 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
