Structure of PDB 1aqy Chain A

Receptor sequence
>1aqyA (length=283) Species: 10090 (Mus musculus) [Search protein sequence]
EYYEVFGEFRGVLMDKRFTKYWEDVEMFLARPDDLVIATYPKSGTTWISE
VVYMIYKEGDVDAIFNRIPYLECRNEDLINGIKQLKEKESPRIVKTHLPP
KLLPASFWEKNCKMIYLCRNAKDVAVSYYYFLLMITSYPNPKSFSEFVEK
FMQGQVPYGSWYDHVKAWWEKSKNSRVLFMFYEDMKEDIRREVVKLIEFL
ERKPSAELVDRIIQHTSFQEMKNNPSTNYTMMPEEMMNQKVSPFMRKGII
GDWKNHFPEALRERFDEHYKQQMKDCTVKFRME
3D structure
PDB1aqy Crystal structure of estrogen sulphotransferase.
ChainA
Resolution1.75 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) K48 H108 S138
Catalytic site (residue number reindexed from 1) K42 H97 S127
Enzyme Commision number 2.8.2.4: estrone sulfotransferase.
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 A3P A K48 G50 T51 T52 W53 R130 S138 Y193 F229 M256 R257 K258 G259 K42 G44 T45 T46 W47 R119 S127 Y182 F218 M245 R246 K247 G248
Gene Ontology
Molecular Function
GO:0004304 estrone sulfotransferase activity
GO:0005496 steroid binding
GO:0008146 sulfotransferase activity
GO:0016740 transferase activity
GO:0050294 steroid sulfotransferase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0007565 female pregnancy
GO:0008210 estrogen metabolic process
GO:0051923 sulfation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1aqy, PDBe:1aqy, PDBj:1aqy
PDBsum1aqy
PubMed9360604
UniProtP49891|ST1E1_MOUSE Sulfotransferase 1E1 (Gene Name=Sult1e1)

[Back to BioLiP]