Structure of PDB 6csb Chain D

Receptor sequence

>6csbD (length=453) Species: 9606 (Homo sapiens) [Search protein sequence]

GKLPPGPQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTH
GEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGL
GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRR
FEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLRFQ
KAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDEN
LRIVVADLFSAGMETTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRR
PEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTT
LITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACL
GEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGVFAFLVSPSPYELCA
VPR

3D structure

PDB

6csb Characteristic conformational changes on the distal and proximal surfaces of cytochrome P450 2D6 in response to substrate binding

Chain

Resolution

2.394 Å

3D
structure

[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

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)
BS01	HEM	D	R101 V119 F120 R132 A305 G306 T309 V374 H376 P435 F436 S437 R441 C443 L444 G445	R57 V75 F76 R88 A261 G262 T265 V330 H332 P391 F392 S393 R397 C399 L400 G401
BS02	RTZ	D	F112 F120 L121 A209 L213 E216 Q244 A300 D301 S304	F68 F76 L77 A165 L169 E172 Q200 A256 D257 S260
BS03	RTZ	D	E222 L372 G373 V374 T375	E178 L328 G329 V330 T331
BS04	ZN	D	H258 D270 E273	H214 D226 E229

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

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:6csb, PDBe:6csb, PDBj:6csb
PDBsum	6csb
PubMed
UniProt	P10635\|CP2D6_HUMAN Cytochrome P450 2D6 (Gene Name=CYP2D6)

[Back to BioLiP]