Structure of PDB 3ua1 Chain A

Receptor sequence
>3ua1A (length=456) Species: 9606 (Homo sapiens) [Search protein sequence]
HSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDG
QQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWK
RLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFG
AYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFP
FLIPILEVLNICVFPREVTNFLRKSVKRMKEEDTQVDFLQLMIDSQHKAL
SDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLP
NKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPK
GVVVMIPSYALHRDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPR
NCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVV
LKVESR
3D structure
PDB3ua1 Structural and Mechanistic Insights into the Interaction of Cytochrome P4503A4 with Bromoergocryptine, a Type I Ligand.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T309 F435 C442
Catalytic site (residue number reindexed from 1) T269 F395 C402
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
1.14.14.55: quinine 3-monooxygenase.
1.14.14.56: 1,8-cineole 2-exo-monooxygenase.
1.14.14.73: albendazole monooxygenase (sufoxide-forming).
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 A R105 S119 W126 R130 F137 F302 A305 G306 T309 T310 R375 P434 F435 R440 N441 C442 I443 A448 R78 S92 W99 R103 F110 F262 A265 G266 T269 T270 R335 P394 F395 R400 N401 C402 I403 A408
BS02 08Y A F57 D76 R105 R106 S119 I120 F215 A305 R372 F30 D49 R78 R79 S92 I93 F188 A265 R332 MOAD: Kd=0.37uM
BindingDB: IC50=2.999E3nM
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005496 steroid binding
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008395 steroid hydroxylase activity
GO:0008401 retinoic acid 4-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:0019825 oxygen binding
GO:0019899 enzyme binding
GO:0020037 heme binding
GO:0030343 vitamin D3 25-hydroxylase activity
GO:0034875 caffeine oxidase activity
GO:0046872 metal ion binding
GO:0050591 quinine 3-monooxygenase activity
GO:0050649 testosterone 6-beta-hydroxylase activity
GO:0062181 1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity
GO:0062187 anandamide 8,9 epoxidase activity
GO:0062188 anandamide 11,12 epoxidase activity
GO:0062189 anandamide 14,15 epoxidase activity
GO:0070330 aromatase activity
GO:0070576 vitamin D 24-hydroxylase activity
GO:0101020 estrogen 16-alpha-hydroxylase activity
GO:0101021 estrogen 2-hydroxylase activity
GO:0102320 1,8-cineole 2-exo-monooxygenase activity
Biological Process
GO:0002933 lipid hydroxylation
GO:0006629 lipid metabolic process
GO:0006631 fatty acid metabolic process
GO:0006694 steroid biosynthetic process
GO:0006706 steroid catabolic process
GO:0006805 xenobiotic metabolic process
GO:0008202 steroid metabolic process
GO:0008203 cholesterol metabolic process
GO:0008209 androgen metabolic process
GO:0008210 estrogen metabolic process
GO:0009822 alkaloid catabolic process
GO:0016098 monoterpenoid metabolic process
GO:0036378 calcitriol biosynthetic process from calciol
GO:0042178 xenobiotic catabolic process
GO:0042359 vitamin D metabolic process
GO:0042369 vitamin D catabolic process
GO:0042572 retinol metabolic process
GO:0042573 retinoic acid metabolic process
GO:0042759 long-chain fatty acid biosynthetic process
GO:0046222 aflatoxin metabolic process
GO:0070989 oxidative demethylation
Cellular Component
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum 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:3ua1, PDBe:3ua1, PDBj:3ua1
PDBsum3ua1
PubMed22157006
UniProtP08684|CP3A4_HUMAN Cytochrome P450 3A4 (Gene Name=CYP3A4)

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