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Literature summary extracted from

  • Becker, J.P.; Depret, G.; Van Bambeke, F.; Tulkens, P.M.; Prevost, M.
    Molecular models of human P-glycoprotein in two different catalytic states (2009), BMC Struct. Biol., 9, 3.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.6.2.2 membrane a transmembrane protein Homo sapiens 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.6.2.2 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

EC Number Organism UniProt Comment Textmining
7.6.2.2 Homo sapiens
-
 gene mdr1 encoding P-gp
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Reaction

EC Number Reaction Comment Organism Reaction ID
7.6.2.2 ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2] P-gp mediated-transport mechanism, overview Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.6.2.2 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
-
 ?
7.6.2.2 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
-
 ?
7.6.2.2 additional information ligand binding structure analysis using the three-dimensional structure modelling, overview Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
7.6.2.2 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

EC Number Synonyms Comment Organism
7.6.2.2 More P-glycoprotein belongs to the family of ATP-binding cassette proteins Homo sapiens
7.6.2.2 P-glycoprotein
-
 Homo sapiens
7.6.2.2 P-gp
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
7.6.2.2 ATP binding and/or hydrolysis of ATP induce conformational changes that are transmitted from the nucleotide binding domains to the transmembrane domains Homo sapiens