Structure of PDB 2vs3 Chain A Binding Site BS03
Receptor Information
>2vs3 Chain A (length=287) Species:
9913
(Bos taurus) [
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KLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGL
TVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPL
RSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQ
DKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHA
AIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHNESHLNKYFLLNKPTK
ILSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVRNNV
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
2vs3 Chain A Residue 403 [
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Receptor-Ligand Complex Structure
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PDB
2vs3
Structural Basis of Udp-Galactose Binding by Alpha- 1,3-Galactosyltransferase (Alpha3Gt): Role of Negative Charge on Aspartic Acid 316 in Structure and Activity.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
D225 D227
Binding residue
(residue number reindexed from 1)
D144 D146
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
Q247 H280 W314 E317 W356 R365
Catalytic site (residue number reindexed from 1)
Q166 H199 W233 E236 W275 R284
Enzyme Commision number
2.4.1.87
: N-acetyllactosaminide 3-alpha-galactosyltransferase.
Gene Ontology
Molecular Function
GO:0016758
hexosyltransferase activity
Biological Process
GO:0005975
carbohydrate metabolic process
Cellular Component
GO:0016020
membrane
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Molecular Function
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Cellular Component
External links
PDB
RCSB:2vs3
,
PDBe:2vs3
,
PDBj:2vs3
PDBsum
2vs3
PubMed
18651752
UniProt
P14769
|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)
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