Structure of PDB 1vzu Chain A Binding Site BS03

Receptor Information
>1vzu Chain A (length=287) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGL
TVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPL
RSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQ
DKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHA
AIFGGTPTQVLNITQECFKGILKDKKNDIEAQYHDESHLNKYFLLNKPTK
ILSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVRNNV
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain1vzu Chain A Residue 1369 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1vzu Roles of active site tryptophans in substrate binding and catalysis by alpha-1,3 galactosyltransferase.
Resolution1.97 Å
Binding residue
(original residue number in PDB)		D225 D227
Binding residue
(residue number reindexed from 1)		D144 D146
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Q247 H280 Y314 E317 W356 R365
Catalytic site (residue number reindexed from 1) Q166 H199 Y233 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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Biological Process
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Cellular Component
External links
PDB RCSB:1vzu, PDBe:1vzu, PDBj:1vzu
PDBsum1vzu
PubMed15229192
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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