Structure of PDB 2vs5 Chain A Binding Site BS01

Receptor Information
>2vs5 Chain A (length=283) 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
IFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDQSHLNKYFLLNKPTKI
LSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVR
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 chain2vs5 Chain A Residue 1366 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2vs5 Structural Basis of Udp-Galactose Binding by Alpha- 1,3-Galactosyltransferase (Alpha3Gt): Role of Negative Charge on Aspartic Acid 316 in Structure and Activity.
Resolution1.82 Å
Binding residue
(original residue number in PDB)
D225 D227
Binding residue
(residue number reindexed from 1)
D143 D145
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Q247 H280 W314 Q317 W356 R365
Catalytic site (residue number reindexed from 1) Q165 H198 W232 Q235 W274 R283
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:2vs5, PDBe:2vs5, PDBj:2vs5
PDBsum2vs5
PubMed18651752
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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