4i4h Summary


Crystal structure of CYP3A4 ligated to pyridine-substituted desoxyritonavir

The structure was published by Sevrioukova, I.F. and Poulos, T.L., in 2013 in a paper entitled "Pyridine-Substituted Desoxyritonavir Is a More Potent Inhibitor of Cytochrome P450 3A4 than Ritonavir." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.9 Å and deposited in 2012.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Cytochrome P450 3A4. This molecule has the UniProt identifier P08684 (CP3A4_HUMAN)search. The sample contained 487 residues which is 96% of the natural sequence. Out of 487 residues 457 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Cytochrome P450 3A4 P08684 (23-503) (CP3A4_HUMAN)search Homo sapienssearch 95% 487 93%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P08684 (23 - 503) Cytochrome P450 3A4 Homo sapiens

Chain Sequence family (Pfam)
A (P08684) PF00067: Cytochrome P450search

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P08684) oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygensearch iron ion bindingsearch heme bindingsearch metal ion bindingsearch taurochenodeoxycholate 6alpha-hydroxylase activitysearch steroid bindingsearch oxidoreductase activitysearch oxygen bindingsearch monooxygenase activitysearch quinine 3-monooxygenase activitysearch caffeine oxidase activitysearch steroid hydroxylase activitysearch vitamin D 24-hydroxylase activitysearch vitamin D3 25-hydroxylase activitysearch testosterone 6-beta-hydroxylase activitysearch albendazole monooxygenase activitysearch enzyme bindingsearch oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygensearch monoterpenoid metabolic processsearch oxidative demethylationsearch xenobiotic metabolic processsearch oxidation-reduction processsearch heterocycle metabolic processsearch vitamin D metabolic processsearch small molecule metabolic processsearch steroid catabolic processsearch drug catabolic processsearch lipid metabolic processsearch alkaloid catabolic processsearch drug metabolic processsearch exogenous drug catabolic processsearch steroid metabolic processsearch androgen metabolic processsearch calcitriol biosynthetic process from calciolsearch intracellular membrane-bounded organellesearch endoplasmic reticulumsearch endoplasmic reticulum membranesearch organelle membranesearch membranesearch cytoplasmsearch integral component of membranesearch

Chain InterPro annotation
A Cytochrome P450search Cytochrome P450, E-class, group IIsearch Cytochrome P450, E-class, CYP3Asearch Cytochrome P450, conserved sitesearch