Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0140359 | molecular_function | ABC-type transporter activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue LTX A 1601 |
| Chain | Residue |
| A | LYS332 |
| A | MET1092 |
| A | ARG1196 |
| A | TYR1242 |
| A | ASN1244 |
| A | TRP1245 |
| A | ARG1248 |
| A | HIS335 |
| A | LEU381 |
| A | PHE385 |
| A | PHE389 |
| A | TYR440 |
| A | TRP553 |
| A | PHE594 |
| A | MET601 |
Functional Information from PROSITE/UniProt
| site_id | PS00211 |
| Number of Residues | 15 |
| Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRVSLARAV |
| Chain | Residue | Details |
| A | LEU768-VAL782 | |
| A | LEU1429-LEU1443 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 415 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 224 |
| Details | Domain: {"description":"ABC transporter 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 27 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O35379","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O35379","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"O35379","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P33527","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
