Structure of PDB 2vfz Chain B Binding Site BS02

Receptor Information
>2vfz Chain B (length=281) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGLT
VFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPLR
SFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQD
KFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHAA
IFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHLNKYFLLNKPTKI
LSPEYCWDYHIGLPADIKLVKMSWQTKEYNV
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 chain2vfz Chain B Residue 2365 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2vfz Conformational Changes Induced by Binding Udp-2F-Galactose to Alpha-1,3 Galactosyltransferase-Implications for Catalysis
Resolution2.4 Å
Binding residue
(original residue number in PDB)		D1225 D1227 K1359
Binding residue
(residue number reindexed from 1)		D143 D145 K277
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Q1247 H1280 W1314 E1317 W1356
Catalytic site (residue number reindexed from 1) Q165 H198 W232 E235 W274
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:2vfz, PDBe:2vfz, PDBj:2vfz
PDBsum2vfz
PubMed17493636
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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