Structure of PDB 2vs4 Chain A Binding Site BS02

Receptor Information
>2vs4 Chain A (length=288) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SKLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVG
LTVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGP
LRSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVF
QDKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYH
AAIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHEESHLNKYFLLNKPT
KILSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVRNNV
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 chain2vs4 Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2vs4 Structural Basis of Udp-Galactose Binding by Alpha- 1,3-Galactosyltransferase (Alpha3Gt): Role of Negative Charge on Aspartic Acid 316 in Structure and Activity.
Resolution1.77 Å
Binding residue
(original residue number in PDB)		D225 D227
Binding residue
(residue number reindexed from 1)		D145 D147
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Q247 H280 W314 E317 W356 R365
Catalytic site (residue number reindexed from 1) Q167 H200 W234 E237 W276 R285
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:2vs4, PDBe:2vs4, PDBj:2vs4
PDBsum2vs4
PubMed18651752
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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