Structure of PDB 3qoa Chain A

Receptor sequence
>3qoaA (length=460) Species: 9606 (Homo sapiens) [Search protein sequence]
GKLPPGPRPLPLLGNLLQMDRRGLLKSFLRFREKYGDVFTVHLGPRPVVM
LCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNRWKVLRRF
SVTTMRDRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIICSI
VFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKHFPGAHR
QVYKNLQEINAYIGHSVEKHRETLDPSAPRDLIDTYLLHMEKEKSNAHSE
FSHQNLNLNTLSLFFAGTETTSTTLRYGFLLMLKYPHVAERVYREIEQVI
GPHRPPELHDRAKMPYTEAVIYEIQRFSDLLPMGVPHIVTQHTSFRGYII
PKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGALKKTEAFIPFSLG
KRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKIPP
TYQIRFLPRH
3D structure
PDB3qoa Structures of Cytochrome P450 2B6 Bound to 4-Benzylpyridine and 4-(4-Nitrobenzyl)pyridine: Insight into Inhibitor Binding and Rearrangement of Active Site Side Chains.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T302 F429 C436
Catalytic site (residue number reindexed from 1) T270 F397 C404
Enzyme Commision number 1.14.13.-
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 R98 W121 R125 A298 T302 L362 L363 H369 P428 F429 S430 R434 C436 L437 G438 R71 W94 R98 A266 T270 L330 L331 H337 P396 F397 S398 R402 C404 L405 G406
BS02 3QO A F297 A298 T302 F265 A266 T270 MOAD: Kd=0.21uM
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008390 testosterone 16-alpha-hydroxylase activity
GO:0008392 arachidonate epoxygenase 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:0020037 heme binding
GO:0046872 metal ion binding
GO:0062184 testosterone 16-beta-hydroxylase activity
GO:0062187 anandamide 8,9 epoxidase activity
GO:0062188 anandamide 11,12 epoxidase activity
GO:0062189 anandamide 14,15 epoxidase activity
GO:0101021 estrogen 2-hydroxylase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0006805 xenobiotic metabolic process
GO:0008202 steroid metabolic process
GO:0019373 epoxygenase P450 pathway
GO:0042178 xenobiotic catabolic process
GO:0042180 cellular ketone metabolic process
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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Cellular Component
External links
PDB RCSB:3qoa, PDBe:3qoa, PDBj:3qoa
PDBsum3qoa
PubMed21875942
UniProtP20813|CP2B6_HUMAN Cytochrome P450 2B6 (Gene Name=CYP2B6)

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