Structure of PDB 4yaf Chain A

Receptor sequence

>4yafA (length=609) Species: 10116 (Rattus norvegicus) [Search protein sequence]

APPVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGM
SADPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETD
VDLTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDG
NLEEDFITWREQFWPAVCEFFGVEASSIRQYELVVHEDMDVAKVYTGEMG
RLKSYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRY
ESGDHVAVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCP
TTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKE
LYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKV
HPNSVHICAVAVEYEAKSGRVNKGVATSWLRAKEPARALVPMFVRKSQFR
LPFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLLYYGCRRS
DEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKL
IHEGGAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTK
GRYSLDVWS

3D structure

PDB

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

Chain

Resolution

1.91 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)	Y392 S393 C561 D606 W608
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	A	S86 Q87 T88 T90 A91 A138 T139 Y140 G141 L173 G174 N175 Y178 H180 F181	S26 Q27 T28 T30 A31 A78 T79 Y80 G81 L113 G114 N115 Y118 H120 F121
BS02	FAD	A	H319 R424 R454 Y455 Y456 S457 A473 V476 Y478 G488 V489 A490 T491 W677	H255 R360 R390 Y391 Y392 S393 A409 V412 Y414 G424 V425 A426 T427 W608
BS03	2AM	A	C566 S596 R597 K602 Y604 Q606 M636	C497 S527 R528 K533 Y535 Q537 M567

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:4yaf, PDBe:4yaf, PDBj:4yaf
PDBsum	4yaf
PubMed	27189945
UniProt	P00388\|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por)

[Back to BioLiP]