Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | a transmembrane protein | Homo sapiens | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + xenobiotic/in | Homo sapiens | P-glycoprotein belongs to the family of ATP-binding cassette proteins which hydrolyze ATP to catalyse the translocation of their substrates through membranes | ADP + phosphate + xenobiotic/out | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
gene mdr1 encoding P-gp | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] | P-gp mediated-transport mechanism, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + xenobiotic/in | P-glycoprotein belongs to the family of ATP-binding cassette proteins which hydrolyze ATP to catalyse the translocation of their substrates through membranes | Homo sapiens | ADP + phosphate + xenobiotic/out | - |
? | |
ATP + H2O + xenobiotic/in | a cluster of aromatic residues located at the interface between the nucleotide binding domain and the transmembrane domain in opposite halves of the molecule may contribute to this signal transmission upon ATP binding and hydrolysis, binding and/or hydrolysis of ATP induce conformational changes that are transmitted from the nucleotide binding domains to the transmembrane domains, overview | Homo sapiens | ADP + phosphate + xenobiotic/out | - |
? | |
additional information | ligand binding structure analysis using the three-dimensional structure modelling, overview | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | three-dimensional models of two different catalytic states of Pglycoprotein are developed based on the crystal structures of two bacterial multidrug transporters, molecular docking, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
More | P-glycoprotein belongs to the family of ATP-binding cassette proteins | Homo sapiens |
P-glycoprotein | - |
Homo sapiens |
P-gp | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | binding and/or hydrolysis of ATP induce conformational changes that are transmitted from the nucleotide binding domains to the transmembrane domains | Homo sapiens |