Structure of PDB 6j7a Chain A

Receptor sequence
>6j7aA (length=814) Species: 10116 (Rattus norvegicus) [Search protein sequence]
SQDLSEALKEATKEVHIRAENSEFMRNFQKGQVSREGFKLVMASLYHIYT
ALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEAIPYTP
ATQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPS
SGEGLAFFTFPSIDNPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLL
NIELFEELQALLPSSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAH
RYGMRGMSADPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFY
DWLQETDVDLTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFEL
GLGDDDGNLEEDFITWREQFWPAVCEFFGVEASSIRQYELVVHEDMDVAK
VYTGEMGRLKSYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDI
SDSKIRYESGDHVAVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNK
KHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMAS
SSGEGKELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYS
IASSSKVHPNSVHICAVAVEYEAKSGRVNKGVATSWLRAKEPALVPMFVR
KSQFRLPFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLLYY
GCRRSDEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDRE
HLWKLIHEGGAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVK
KLMTKGRYSLDVWS
3D structure
PDB6j7a Crystal structure of a NADPH-cytochrome P450 oxidoreductase (CYPOR) and heme oxygenase 1 fusion protein implies a conformational change in CYPOR upon NADPH/NADP+binding.
ChainA
Resolution3.269 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S634 C807 D852 W854
Catalytic site (residue number reindexed from 1) S600 C766 D811 W813
Enzyme Commision number 1.14.14.18: heme oxygenase (biliverdin-producing).
1.6.2.4: NADPH--hemoprotein reductase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003958 NADPH-hemoprotein reductase activity
GO:0004128 cytochrome-b5 reductase activity, acting on NAD(P)H
GO:0004392 heme oxygenase (decyclizing) activity
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:0006788 heme oxidation
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:6j7a, PDBe:6j7a, PDBj:6j7a
PDBsum6j7a
PubMed30883732
UniProtP00388|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por);
P06762|HMOX1_RAT Heme oxygenase 1 (Gene Name=Hmox1)

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