Structure of PDB 1aqu Chain B

Receptor sequence
>1aquB (length=280) Species: 10090 (Mus musculus) [Search protein sequence]
EYYEVFGEFRGVLMDKRFTKYWEDVEMFLARPDDLVIATYPKSGTTWISE
VVYMIYKEEDAIFNRIPYLECRNEDLINGIKQLKEKESPRIVKTHLPPKL
LPASFWEKNCKMIYLCRNAKDVAVSYYYFLLMITSYPNPKSFSEFVEKFM
QGQVPYGSWYDHVKAWWEKSKNSRVLFMFYEDMKEDIRREVVKLIEFLER
KPSAELVDRIIQHTSFQEMKNNPSTNYTMMPEEMMNQKVSPFMRKGIIGD
WKNHFPEALRERFDEHYKQQMKDCTVKFRM
3D structure
PDB1aqu Crystal structure of estrogen sulphotransferase.
ChainB
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K48 H108 S138
Catalytic site (residue number reindexed from 1) K42 H95 S125
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 B K48 G50 T51 T52 W53 R130 S138 Y193 F229 M256 R257 G259 K42 G44 T45 T46 W47 R117 S125 Y180 F216 M243 R244 G246
BS02 EST B R23 Y81 K106 F142 M247 R17 Y68 K93 F129 M234
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1aqu, PDBe:1aqu, PDBj:1aqu
PDBsum1aqu
PubMed9360604
UniProtP49891|ST1E1_MOUSE Sulfotransferase 1E1 (Gene Name=Sult1e1)

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