Structure of PDB 3rx2 Chain A
Receptor sequence
>3rx2A (length=318) Species:
9606
(Homo sapiens) [
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SHMASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHV
YQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLS
DLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEEL
VDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQ
YCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQV
LIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRV
CALLSCTSHKDYPFHEEF
3D structure
PDB
3rx2
The molecular basis for inhibition of sulindac and its metabolites towards human aldose reductase
Chain
A
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)
P23 D43 Y48 K77 H110
Catalytic site (residue number reindexed from 1)
P26 D46 Y51 K80 H113
Enzyme Commision number
1.1.1.21
: aldose reductase.
1.1.1.300
: NADP-retinol dehydrogenase.
1.1.1.372
: D/L-glyceraldehyde reductase.
1.1.1.54
: allyl-alcohol dehydrogenase.
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
NAP
A
G18 T19 W20 D43 Y48 H110 N160 Q183 Y209 S210 P211 L212 S214 P215 D216 A245 I260 P261 K262 S263 V264 T265 R268 E271 N272 C298
G21 T22 W23 D46 Y51 H113 N163 Q186 Y212 S213 P214 L215 S217 P218 D219 A248 I263 P264 K265 S266 V267 T268 R271 E274 N275 C301
BS02
SLO
A
W20 Y48 H110 W111 F122 W219 C298 S302
W23 Y51 H113 W114 F125 W222 C301 S305
Gene Ontology
Molecular Function
GO:0001758
retinal dehydrogenase activity
GO:0004032
aldose reductase (NADPH) activity
GO:0005515
protein binding
GO:0009055
electron transfer activity
GO:0016491
oxidoreductase activity
GO:0036130
prostaglandin H2 endoperoxidase reductase activity
GO:0043795
glyceraldehyde oxidoreductase activity
GO:0047655
allyl-alcohol dehydrogenase activity
GO:0047939
L-glucuronate reductase activity
GO:0047956
glycerol dehydrogenase (NADP+) activity
GO:0052650
all-trans-retinol dehydrogenase (NADP+) activity
Biological Process
GO:0001523
retinoid metabolic process
GO:0002070
epithelial cell maturation
GO:0003091
renal water homeostasis
GO:0005975
carbohydrate metabolic process
GO:0006629
lipid metabolic process
GO:0006693
prostaglandin metabolic process
GO:0006700
C21-steroid hormone biosynthetic process
GO:0019853
L-ascorbic acid biosynthetic process
GO:0035809
regulation of urine volume
GO:0042572
retinol metabolic process
GO:0043066
negative regulation of apoptotic process
GO:0044597
daunorubicin metabolic process
GO:0044598
doxorubicin metabolic process
GO:0046370
fructose biosynthetic process
GO:0071475
cellular hyperosmotic salinity response
GO:0072205
metanephric collecting duct development
Cellular Component
GO:0005615
extracellular space
GO:0005654
nucleoplasm
GO:0005737
cytoplasm
GO:0005739
mitochondrion
GO:0005829
cytosol
GO:0070062
extracellular exosome
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:3rx2
,
PDBe:3rx2
,
PDBj:3rx2
PDBsum
3rx2
PubMed
22155003
UniProt
P15121
|ALDR_HUMAN Aldo-keto reductase family 1 member B1 (Gene Name=AKR1B1)
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