Structure of PDB 5uri Chain B

Receptor sequence

>5uriB (length=602) Species: 10116 (Rattus norvegicus) [Search protein sequence]

SSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEE
YDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVDLTGV
KFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDF
ITWREQFWPAVCEFFGVEASIRQYELVVHEDMDVAKVYTGEMGRLKSYEN
QKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRYESGDHVA
VYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRTAL
TYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKELYLSWVV
EARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHI
CAVAVEYEAKSGRVNKGVATSWLRAKEPAGRALVPMFVRKSQFRLPFKST
TPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLLYYGCRRSDEDYLY
REELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKLIHEGGA
HIYVCGAANMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDV
WS

3D structure

PDB

5uri Structural and Kinetic Studies of Asp632 Mutants and Fully Reduced NADPH-Cytochrome P450 Oxidoreductase Define the Role of Asp632 Loop Dynamics in the Control of NADPH Binding and Hydride Transfer.

Chain

Resolution

2.7 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	S457 C630 D675 W677
Catalytic site (residue number reindexed from 1)	S386 C555 D599 W601
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 G141 G143 G174 N175 Y178 H180 D208	S20 Q21 T22 T24 A25 T73 Y74 G75 G77 G108 N109 Y112 H114 D142
BS02	FAD	B	R424 R454 Y455 Y456 S457 C472 A473 V476 Y478 G488 V489 A490 T491 W677	R353 R383 Y384 Y385 S386 C401 A402 V405 Y407 G417 V418 A419 T420 W601
BS03	2AM	B	G534 C566 S596 R597 K602 Y604 Q606 M636	G459 C491 S521 R522 K527 Y529 Q531 M560

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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Biological Process

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Cellular Component

External links

PDB	RCSB:5uri, PDBe:5uri, PDBj:5uri
PDBsum	5uri
PubMed	29308883
UniProt	P00388\|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por)

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