Structure of PDB 2acr Chain A
Receptor sequence
>2acrA (length=315) Species:
9606
(Homo sapiens) [
Search protein sequence
]
ASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQN
ENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLK
LDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDE
GLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQ
SKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIR
FPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCAL
LSCTSHKDYPFHEEF
3D structure
PDB
2acr
An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate.
Chain
A
Resolution
1.76 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)
D43 Y48 K77 H110
Catalytic site (residue number reindexed from 1)
D43 Y48 K77 H110
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
CAC
A
W20 Y48 H110
W20 Y48 H110
BS02
NAP
A
G18 T19 W20 K21 D43 Y48 H110 Q183 Y209 S210 P211 L212 S214 P215 D216 A245 I260 P261 K262 S263 V264 T265 R268 E271 N272
G18 T19 W20 K21 D43 Y48 H110 Q183 Y209 S210 P211 L212 S214 P215 D216 A245 I260 P261 K262 S263 V264 T265 R268 E271 N272
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:2acr
,
PDBe:2acr
,
PDBj:2acr
PDBsum
2acr
PubMed
8117658
UniProt
P15121
|ALDR_HUMAN Aldo-keto reductase family 1 member B1 (Gene Name=AKR1B1)
[
Back to BioLiP
]