Structure of PDB 3ua5 Chain B

Receptor sequence

>3ua5B (length=462) Species: 9606 (Homo sapiens) [Search protein sequence]

KLPPGPRPLPLLGNLLQMDRRGLLKSFLRFREKYGDVFTVHLGPRPVVML
CGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNRWKVLRRFS
VTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANI
ICSIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKHFP
GAHRQVYKNLQEINAYIGHSVEKHRETLDPSAPRDLIDTYLLHMEKEKSN
AEFSHQNLNLNTLSLFFAGTETTSTTLRYGFLLMLKYPHVAERVYREIEQ
VIGPHRPPELHDRAKMPYTEAVIYEIQRFSDLLPMGVPHIVTQHTSFRGY
IIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGALKKTEAFIPFS
LGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKI
PPTYQIRFLPRH

3D structure

PDB

3ua5 Conformational Adaptation of Human Cytochrome P450 2B6 and Rabbit Cytochrome P450 2B4 Revealed upon Binding Multiple Amlodipine Molecules.

Chain

Resolution

2.8 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)	T272 F399 C406
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)
BS01	HEM	B	R98 V113 I114 W121 R125 G299 T302 L362 H369 F429 S430 R434 C436 L437 G438	R70 V85 I86 W93 R97 G269 T272 L332 H339 F399 S400 R404 C406 L407 G408
BS02	06X	B	I101 F206 S210 F297 A298 V477	I73 F178 S182 F267 A268 V447
BS03	06X	B	L51 Q215 E218 F389 G476 V477	L23 Q187 E190 F359 G446 V447

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

View graph for
Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:3ua5, PDBe:3ua5, PDBj:3ua5
PDBsum	3ua5
PubMed	22909231
UniProt	P20813\|CP2B6_HUMAN Cytochrome P450 2B6 (Gene Name=CYP2B6)

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