Structure of PDB 4wnt Chain A

Receptor sequence

>4wntA (length=457) Species: 9606 (Homo sapiens) [Search protein sequence]

GKLPPGPLPDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREA
LVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLR
NLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLT
CGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV
LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSF
NDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIG
QVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIP
KGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGR
RACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGVFAFLVSPSPY
ELCAVPR

3D structure

PDB

4wnt Contributions of Ionic Interactions and Protein Dynamics to Cytochrome P450 2D6 (CYP2D6) Substrate and Inhibitor Binding.

Chain

Resolution

2.6 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 F436 C443
Catalytic site (residue number reindexed from 1)	T269 F396 C403
Enzyme Commision number	1.14.14.-

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	R101 V119 F120 W128 R132 A305 T309 H376 P435 F436 S437 R441 C443 L444 G445 L448	R61 V79 F80 W88 R92 A265 T269 H336 P395 F396 S397 R401 C403 L404 G405 L408
BS02	AJN	A	L110 F120 A209 L213 E216 Q244 F247 D301 S304 A305 F483	L70 F80 A169 L173 E176 Q204 F207 D261 S264 A265 F443	BindingDB: Ki=4.6nM
BS03	ZN	A	H258 D270 E273	H218 D230 E233
BS04	ZN	A	D422 H426	D382 H386

Gene Ontology

	Molecular Function
GO:0004497	monooxygenase activity
GO:0005506	iron ion binding
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:0020037	heme binding
GO:0046872	metal ion binding
GO:0062187	anandamide 8,9 epoxidase activity
GO:0062188	anandamide 11,12 epoxidase activity
GO:0062189	anandamide 14,15 epoxidase activity

	Biological Process
GO:0006631	fatty acid metabolic process
GO:0006805	xenobiotic metabolic process
GO:0008202	steroid metabolic process
GO:0008203	cholesterol metabolic process
GO:0008210	estrogen metabolic process
GO:0009804	coumarin metabolic process
GO:0009820	alkaloid metabolic process
GO:0009822	alkaloid catabolic process
GO:0016098	monoterpenoid metabolic process
GO:0019369	arachidonate metabolic process
GO:0033076	isoquinoline alkaloid metabolic process
GO:0042178	xenobiotic catabolic process
GO:0042572	retinol metabolic process
GO:0042759	long-chain fatty acid biosynthetic process
GO:0051100	negative regulation of binding
GO:0070989	oxidative demethylation
GO:0090350	negative regulation of cellular organofluorine metabolic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005739	mitochondrion
GO:0005783	endoplasmic reticulum
GO:0005789	endoplasmic reticulum membrane
GO:0016020	membrane
GO:0043231	intracellular membrane-bounded organelle

View graph for
Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:4wnt, PDBe:4wnt, PDBj:4wnt
PDBsum	4wnt
PubMed	25555909
UniProt	P10635\|CP2D6_HUMAN Cytochrome P450 2D6 (Gene Name=CYP2D6)

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