Structure of PDB 1bo6 Chain B

Receptor sequence
>1bo6B (length=282) Species: 10090 (Mus musculus) [Search protein sequence]
EYYEVFGEFRGVLMDKRFTKYWEDVEMFLARPDDLVIATYPKSGTTWISE
VVYMIYKEKEDAIFNRIPYLECRNEDLINGIKQLKEKESPRIVKTHLPPK
LLPASFWEKNCKMIYLCRNAKDVAVSYYYFLLMITSYPNPKSFSEFVEKF
MQGQVPYGSWYDHVKAWWEKSKNSRVLFMFYEDMKEDIRREVVKLIEFLE
RKPSAELVDRIIQHTSFQEMKNNPSTNYTMMPEEMMNQKVSPFMRKGIIG
DWKNHFPEALRERFDEHYKQQMKDCTVKFRME
3D structure
PDB1bo6 The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis.
ChainB
Resolution2.1 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 H96 S126
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 VO4 B P47 K48 T51 K106 H108 F255 P41 K42 T45 K94 H96 F243
BS02 A3P B K48 G50 T51 T52 W53 R130 S138 Y193 F229 M232 M256 R257 K258 G259 K42 G44 T45 T46 W47 R118 S126 Y181 F217 M220 M244 R245 K246 G247
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:1bo6, PDBe:1bo6, PDBj:1bo6
PDBsum1bo6
PubMed9765259
UniProtP49891|ST1E1_MOUSE Sulfotransferase 1E1 (Gene Name=Sult1e1)

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