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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 PDB 1aqu Crystal structure of estrogen sulphotransferase. Chain B Resolution 1.6 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 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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