Structure of PDB 4y9r Chain B

Receptor sequence

>4y9rB (length=605) Species: 10116 (Rattus norvegicus) [Search protein sequence]

PVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSA
DPEEYDLADLSSLPEIDKSLVVFCMATYEGDPTDNAQDFYDWLQETDVDL
TGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLE
EDFITWREQFWPAVCEFFGVEATSIRQYELVVHEDMDVAKVYTGEMGRLK
SYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRYESG
DHVAVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTY
RTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKELYL
SWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPN
SVHICAVAVEYEAKSGRVNKGVATSWLRAKEPRALVPMFVRKSQFRLPFK
STTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLLYYGCRRSDEDY
LYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKLIHEG
GAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYS
LDVWS

3D structure

PDB

4y9r Mutants of Cytochrome P450 Reductase Lacking Either Gly-141 or Gly-143 Destabilize Its FMN Semiquinone.

Chain

Resolution

2.4 Å

3D
structure

Catalytic site residues are labeled in the 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

Catalytic site (original residue number in PDB)	Y456 S457 C630 D675 W677
Catalytic site (residue number reindexed from 1)	Y389 S390 C557 D602 W604
Enzyme Commision number	1.6.2.4: NADPH--hemoprotein reductase.

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	FMN	B	S86 Q87 T88 T90 A91 T139 Y140 E142 L173 G174 N175 Y178 H180	S24 Q25 T26 T28 A29 T77 Y78 E79 L110 G111 N112 Y115 H117
BS02	FAD	B	H319 R424 R454 Y455 Y456 S457 C472 A473 V474 Y478 G488 V489 A490 T491 W677	H252 R357 R387 Y388 Y389 S390 C405 A406 V407 Y411 G421 V422 A423 T424 W604
BS03	NAP	B	R298 G534 T535 C566 S596 R597 K602 Y604 Q606	R231 G461 T462 C493 S523 R524 K529 Y531 Q533

Gene Ontology

	Molecular Function
GO:0003958	NADPH-hemoprotein reductase activity
GO:0004128	cytochrome-b5 reductase activity, acting on NAD(P)H
GO:0008941	nitric oxide dioxygenase NAD(P)H activity
GO:0009055	electron transfer activity
GO:0010181	FMN binding
GO:0016491	oxidoreductase activity
GO:0016787	hydrolase activity
GO:0019899	enzyme binding
GO:0047726	iron-cytochrome-c reductase activity
GO:0050660	flavin adenine dinucleotide binding
GO:0050661	NADP binding

	Biological Process
GO:0003420	regulation of growth plate cartilage chondrocyte proliferation
GO:0007584	response to nutrient
GO:0009410	response to xenobiotic stimulus
GO:0009437	carnitine metabolic process
GO:0009725	response to hormone
GO:0009812	flavonoid metabolic process
GO:0019395	fatty acid oxidation
GO:0022900	electron transport chain
GO:0032332	positive regulation of chondrocyte differentiation
GO:0043066	negative regulation of apoptotic process
GO:0043602	nitrate catabolic process
GO:0045542	positive regulation of cholesterol biosynthetic process
GO:0045880	positive regulation of smoothened signaling pathway
GO:0046210	nitric oxide catabolic process
GO:0070988	demethylation
GO:0071371	cellular response to gonadotropin stimulus
GO:0071372	cellular response to follicle-stimulating hormone stimulus
GO:0071375	cellular response to peptide hormone stimulus
GO:0071548	response to dexamethasone
GO:0090031	positive regulation of steroid hormone biosynthetic process
GO:0090181	regulation of cholesterol metabolic process
GO:0090346	cellular organofluorine metabolic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005783	endoplasmic reticulum
GO:0005789	endoplasmic reticulum membrane
GO:0005829	cytosol
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:4y9r, PDBe:4y9r, PDBj:4y9r
PDBsum	4y9r
PubMed	27189945
UniProt	P00388\|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por)

[Back to BioLiP]