Structure of PDB 5urg Chain B
Receptor sequence
>5urgB (length=604) Species:
10116
(Rattus norvegicus) [
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SSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEE
YDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVDLTGV
KFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDF
ITWREQFWPAVCEFFGVEATSSIRQYELVVHEDMDVAKVYTGEMGRLKSY
ENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRYESGDH
VAVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRT
ALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKELYLSW
VVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSV
HICAVAVEYEAKSGRVNKGVATSWLRAKEPARALVPMFVRKSQFRLPFKS
TTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLLYYGCRRSDEDYL
YREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKLIHEGG
AHIYVCGFARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSL
DVWS
3D structure
PDB
5urg
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
2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB)
S457 C630 D675 W677
Catalytic site (residue number reindexed from 1)
S388 C556 D601 W603
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 G141 L173 G174 N175 Y178 H180 F181
S20 Q21 T22 T24 A25 T73 Y74 G75 L107 G108 N109 Y112 H114 F115
BS02
FAD
B
H319 R454 Y455 Y456 S457 C472 A473 Y478 G488 V489 A490 T491 F632 W677
H250 R385 Y386 Y387 S388 C403 A404 Y409 G419 V420 A421 T422 F558 W603
BS03
NAP
B
R298 G534 T535 C566 R567 S596 R597 K602 Y604 Q606 F632
R229 G460 T461 C492 R493 S522 R523 K528 Y530 Q532 F558
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:5urg
,
PDBe:5urg
,
PDBj:5urg
PDBsum
5urg
PubMed
29308883
UniProt
P00388
|NCPR_RAT NADPH--cytochrome P450 reductase (Gene Name=Por)
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