Structure of PDB 5urd Chain B
Receptor sequence
>5urdB (length=605) Species:
10116
(Rattus norvegicus) [
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VKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSAD
PEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVDL
TGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLE
EDFITWREQFWPAVCEFFGVEATIRQYELVVHEDMDVAKVYTGEMGRLKS
YENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRYESGD
HVAVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYR
TALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKELYLS
WVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNS
VHICAVAVEYEAKSGRVNKGVATSWLRAKEPARALVPMFVRKSQFRLPFK
STTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLLYYGCRRSDEDY
LYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKLIHEG
GAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYS
LDVWS
3D structure
PDB
5urd
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
B
Resolution
1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB)
Y456 S457 C630 D675 W677
Catalytic site (residue number reindexed from 1)
Y388 S389 C557 D602 W604
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
B
S86 Q87 T88 T90 A91 T139 Y140 G143 L173 G174 N175 Y178 H180
S23 Q24 T25 T27 A28 T76 Y77 G80 L110 G111 N112 Y115 H117
BS02
FAD
B
H319 R424 R454 Y455 Y456 S457 C472 A473 V476 Y478 G488 V489 A490 T491 W677
H251 R356 R386 Y387 Y388 S389 C404 A405 V408 Y410 G420 V421 A422 T423 W604
BS03
NAP
B
R298 G534 T535 C566 S596 R597 K602 Y604 Q606 M636
R230 G461 T462 C493 S523 R524 K529 Y531 Q533 M563
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:5urd
,
PDBe:5urd
,
PDBj:5urd
PDBsum
5urd
PubMed
29308883
UniProt
P00388
|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por)
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