Structure of PDB 1ja0 Chain B
Receptor sequence
>1ja0B (length=432) Species:
10116
(Rattus norvegicus) [
Search protein sequence
]
IRQYELVVHEDMDVAKVYTGEMGRLKSYENQKPPFDAKNPFLAAVTANRK
LNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSALVNQIGEILGAD
LDVIMSLNNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQ
YASEPSEQEHLHKMASSSGEGKELYLSWVVEARRHILAILQDYPSLRPPI
DHLCELLPRLQARYYSIASSSKVHPNSVHICAVAVEYEAKSGRVNKGVAT
SWLRAKEPAGGRALVPMFVRKSQFRLPFKSTTPVIMVGPGTGIAPFMGFI
QERAWLREQGKEVGETLLYYGCRRSDEDYLYREELARFHKDGALTQLNVA
FSREQAHKVYVQHLLKRDREHLWKLIHEGGAHIYVCGDARNMAKDVQNTF
YDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDV
3D structure
PDB
1ja0
NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer.
Chain
B
Resolution
2.6 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 S457 C630 D675
Catalytic site (residue number reindexed from 1)
Y215 S216 C386 D431
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
H319 R424 R454 Y455 Y456 S457 C472 A473 V476 Y478 G488 V489 A490 T491
H78 R183 R213 Y214 Y215 S216 C231 A232 V235 Y237 G247 V248 A249 T250
BS02
NAP
B
R298 G534 T535 C566 S596 R597 K602 Y604 Q606 C630 G631 M636 D639 D675 V676
R57 G290 T291 C322 S352 R353 K358 Y360 Q362 C386 G387 M392 D395 D431 V432
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:1ja0
,
PDBe:1ja0
,
PDBj:1ja0
PDBsum
1ja0
PubMed
11371558
UniProt
P00388
|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por)
[
Back to BioLiP
]