8OX4
Cryo-EM structure of ATP8B1-CDC50A in E1-ATP conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005215 | molecular_function | transporter activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0015914 | biological_process | phospholipid transport |
| A | 0016020 | cellular_component | membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0140326 | molecular_function | ATPase-coupled intramembrane lipid transporter activity |
| B | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00154 |
| Number of Residues | 7 |
| Details | ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT |
| Chain | Residue | Details |
| A | ASP454-THR460 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 61 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| B | ALA2-THR49 | |
| B | ASN347-ILE361 | |
| A | ARG412-LYS949 | |
| A | LEU1003-ARG1032 | |
| A | THR1092-PHE1097 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| B | VAL50-VAL70 | |
| A | ALA1139-ILE1163 | |
| B | GLY326-ILE346 | |
| A | VAL341-TRP362 | |
| A | TRP390-ILE411 | |
| A | PHE950-PHE970 | |
| A | TRP983-LEU1002 | |
| A | PHE1033-ALA1054 | |
| A | TYR1069-ASP1091 | |
| A | VAL1098-HIS1118 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 254 |
| Details | TOPO_DOM: Exoplasmic loop => ECO:0000255 |
| Chain | Residue | Details |
| B | THR71-LEU325 | |
| A | GLU363-PHE389 | |
| A | PHE971-ASP982 | |
| A | TYR1055-ASP1068 | |
| A | SER1119-ASN1138 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
| Chain | Residue | Details |
| B | ALA2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31416931, ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, ECO:0007744|PDB:6K7M |
| Chain | Residue | Details |
| B | ASN107 | |
| A | LYS455 | |
| A | THR456 | |
| A | PHE596 | |
| A | ASN896 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:31416931, ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, ECO:0007744|PDB:6K7M |
| Chain | Residue | Details |
| B | ASN180 | |
| A | LYS619 | |
| A | ARG652 | |
| A | THR732 | |
| A | GLY733 | |
| A | ASP734 | |
| A | ARG867 | |
| A | LYS873 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 |
| Chain | Residue | Details |
| B | ASN190 | |
| A | ASP897 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:31416931, ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, ECO:0007744|PDB:6K7M |
| Chain | Residue | Details |
| B | ASN294 |
