Structure of PDB 3wkt Chain B
Receptor sequence
>3wktB (length=588) Species:
10116
(Rattus norvegicus) [
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VEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSSSLPEIDK
SLVVFCMATYGEGDPTDNAQDFYDWLQETDVDLTGVKFAVFGLGNKTYEH
FNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEF
FGVEASSIRQYELVVHEDMDVAKVYTGEMGRLKSYENQKPPFDAKNPFLA
AVTANRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSALVNQI
GEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTN
VLYELAQYASEPSEQEHLHKMASSSGEGKELYLSWVVEARRHILAILQDY
PSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVAVEYEAKSGR
VNKGVATSWLRAKEPRALVPMFVRKSQFRLPFKSTTPVIMVGPGTGIAPF
MGFIQERAWLREQGKEVGETLLYYGCRRSDEDYLYREELARFHKDGALTQ
LNVAFSREQAHKVYVQHLLKRDREHLWKLIHEGGAHIYVCGDARNMAKDV
QNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDVWS
3D structure
PDB
3wkt
Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.
Chain
B
Resolution
4.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB)
Y452 S453 C626 D671 W673
Catalytic site (residue number reindexed from 1)
Y372 S373 C540 D585 W587
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
FAD
B
H315 R420 R450 Y451 Y452 S453 C468 A469 V472 Y474 G484 A486 T487 W673
H235 R340 R370 Y371 Y372 S373 C388 A389 V392 Y394 G404 A406 T407 W587
BS02
FMN
B
S86 Q87 T88 T90 A91 T139 Y140 G141 L173 G174 N175 Y178 H180 F181
S17 Q18 T19 T21 A22 T59 Y60 G61 L93 G94 N95 Y98 H100 F101
BS03
NAP
B
R294 C562 S592 R593 K598 Y600 V601 Q602 M632
R214 C476 S506 R507 K512 Y514 V515 Q516 M546
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:3wkt
,
PDBe:3wkt
,
PDBj:3wkt
PDBsum
3wkt
PubMed
24550278
UniProt
P00388
|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por)
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