Structure of PDB 7l18 Chain AAA
Receptor sequence
>7l18AAA (length=606) Species:
10116
(Rattus norvegicus) [
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PVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSA
DPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVD
LTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNL
EEDFITWREQFWPAVCEFFGVEATSSIRQYELVVHEDMDVAKVYTGEMGR
LKSYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRYE
SGDHVAVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPT
TYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKEL
YLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVH
PNSVHICAVAVEYEAKSGRVNKGVATSWLRAKEPGRALVPMFVRKSQFRL
PFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLLYYGCRRSD
EDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKLI
HEGGAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKG
RYSLWS
3D structure
PDB
7l18
Structural and kinetic investigations of the carboxy terminus of NADPH-cytochrome P450 oxidoreductase.
Chain
AAA
Resolution
2.542 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 W677
Catalytic site (residue number reindexed from 1)
S392 C560 W605
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)
Binding affinity
BS01
FMN
AAA
S86 Q87 T88 T90 A91 A138 T139 Y140 G141 G143 G174 N175 Y178 H180 F181
S24 Q25 T26 T28 A29 A76 T77 Y78 G79 G81 G112 N113 Y116 H118 F119
BS02
FAD
AAA
R424 R454 Y455 Y456 S457 C472 A473 Y478 G488 V489 A490 T491 W677
R359 R389 Y390 Y391 S392 C407 A408 Y413 G423 V424 A425 T426 W605
BS03
NAP
AAA
R298 G534 T535 C566 S596 R597 K602 Y604 Q606 M636
R233 G464 T465 C496 S526 R527 K532 Y534 Q536 M566
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:7l18
,
PDBe:7l18
,
PDBj:7l18
PDBsum
7l18
PubMed
33556357
UniProt
P00388
|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por)
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