Structure of PDB 4gqs Chain D

Receptor sequence
>4gqsD (length=452) Species: 9606 (Homo sapiens) [Search protein sequence]
LPPGPTPLPVIGNILQIDIKDVSKSLTNLSKIYGPVFTLYFGLERMVVLH
GYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRWKEIRRFSL
MTLEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFQKRFD
YKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLA
FMESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLV
ITAADLLGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVVGRNRSPC
MQDRGHMPYTDAVVHEVQRYIDLIPTSLPHAVTCDVKFRNYLIPKGTTIL
TSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFKKSNYFMPFSAGKRICVGE
GLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVPPFYQLCFI
PI
3D structure
PDB4gqs Structural Characterization of Human Cytochrome P450 2C19: ACTIVE SITE DIFFERENCES BETWEEN P450s 2C8, 2C9, AND 2C19.
ChainD
Resolution2.87 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T301 F428 C435
Catalytic site (residue number reindexed from 1) T263 F390 C397
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
1.14.14.51: (S)-limonene 6-monooxygenase.
1.14.14.52: (S)-limonene 7-monooxygenase.
1.14.14.53: (R)-limonene 6-monooxygenase.
1.14.14.75: fenbendazole monooxygenase (4'-hydroxylating).
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 HEM D R97 I112 V113 W120 R124 L294 A297 G298 T301 T302 I362 H368 F428 S429 R433 C435 G437 A441 R69 I84 V85 W92 R96 L256 A259 G260 T263 T264 I324 H330 F390 S391 R395 C397 G399 A403
BS02 0XV D F114 A297 I362 L366 F86 A259 I324 L328
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008392 arachidonate epoxygenase activity
GO:0008395 steroid hydroxylase activity
GO:0016491 oxidoreductase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016712 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 oxygen
GO:0018675 (S)-limonene 6-monooxygenase activity
GO:0018676 (S)-limonene 7-monooxygenase activity
GO:0019825 oxygen binding
GO:0019899 enzyme binding
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0052741 (R)-limonene 6-monooxygenase activity
GO:0070330 aromatase activity
GO:0120319 long-chain fatty acid omega-1 hydroxylase activity
Biological Process
GO:0001676 long-chain fatty acid metabolic process
GO:0006631 fatty acid metabolic process
GO:0006805 xenobiotic metabolic process
GO:0008202 steroid metabolic process
GO:0016098 monoterpenoid metabolic process
GO:0019373 epoxygenase P450 pathway
GO:0042178 xenobiotic catabolic process
GO:0097267 omega-hydroxylase P450 pathway
Cellular Component
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4gqs, PDBe:4gqs, PDBj:4gqs
PDBsum4gqs
PubMed23118231
UniProtP33261|CP2CJ_HUMAN Cytochrome P450 2C19 (Gene Name=CYP2C19)

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