Structure of PDB 1ja0 Chain A

Receptor sequence

>1ja0A (length=607) Species: 10116 (Rattus norvegicus) [Search protein sequence]

PVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSA
DPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVD
LTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNL
EEDFITWREQFWPAVCEFFGVEATGEESSIRQYELVVHEDMDVAKVYTGE
MGRLKSYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKI
RYESGDHVAVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFP
CPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEG
KELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSS
KVHPNSVHICAVAVEYEAKSGRVNKGVATSWLRAKEPALVPMFVRKSQFR
LPFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLLYYGCRRS
DEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKL
IHEGGAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTK
GRYSLDV

3D structure

PDB

1ja0 NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer.

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)	Y456 S457 C630 D675
Catalytic site (residue number reindexed from 1)	Y394 S395 C561 D606
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	FAD	A	H319 R424 R454 Y455 Y456 S457 C472 A473 V474 V476 Y478 G488 V489 A490 T491	H257 R362 R392 Y393 Y394 S395 C410 A411 V412 V414 Y416 G426 V427 A428 T429
BS02	FMN	A	S86 Q87 T88 T90 A91 T139 Y140 L173 G174 N175 Y178 H180 D208	S24 Q25 T26 T28 A29 T77 Y78 L111 G112 N113 Y116 H118 D146
BS03	NAP	A	R298 G534 T535 C566 S596 R597 K602 Y604 Q606 G631 N635 M636 D639 D675 V676	R236 G465 T466 C497 S527 R528 K533 Y535 Q537 G562 N566 M567 D570 D606 V607

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

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Molecular Function

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Cellular Component

External links

PDB	RCSB:1ja0, PDBe:1ja0, PDBj:1ja0
PDBsum	1ja0
PubMed	11371558
UniProt	P00388\|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por)

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