Structure of PDB 1ja1 Chain A

Receptor sequence

>1ja1A (length=616) Species: 10116 (Rattus norvegicus) [Search protein sequence]

PVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSA
DPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVD
LTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNL
EEDFITWREQFWPAVCEFFGVEATGEESSIRQYELVVHEDMDVAKVYTGE
MGRLKSYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKI
RYESGDHVAVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFP
CPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEG
KELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYAIASSS
KVHPNSVHICAVAVEYEAKSGRVNKGVATSWLRAKEPAGENGGRALVPMF
VRKSQFRLPFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLL
YYGCRRSDEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRD
REHLWKLIHEGGAHIYVAGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDY
VKKLMTKGRYSLNVWS

3D structure

PDB

1ja1 NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer.

Chain

Resolution

1.8 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 A457 A630 N675 W677
Catalytic site (residue number reindexed from 1)	Y394 A395 A568 N613 W615
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 R454 Y455 Y456 A457 C472 A473 V476 Y478 G488 V489 A490 T491 W677	H257 R392 Y393 Y394 A395 C410 A411 V414 Y416 G426 V427 A428 T429 W615
BS02	FMN	A	S86 Q87 T88 T90 A91 A138 T139 Y140 L173 G174 Y178 F181 D208	S24 Q25 T26 T28 A29 A76 T77 Y78 L111 G112 Y116 F119 D146
BS03	NAP	A	R298 G534 T535 C566 R567 S596 R597 K602 Y604 Q606 N635 M636 S678	R236 G472 T473 C504 R505 S534 R535 K540 Y542 Q544 N573 M574 S616

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:1ja1, PDBe:1ja1, PDBj:1ja1
PDBsum	1ja1
PubMed	11371558
UniProt	P00388\|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por)

[Back to BioLiP]