Structure of PDB 2vs5 Chain A Binding Site BS01
Receptor Information
>2vs5 Chain A (length=283) Species:
9913
(Bos taurus) [
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LKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGLT
VFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPLR
SFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQD
KFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHAA
IFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDQSHLNKYFLLNKPTKI
LSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVR
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
2vs5 Chain A Residue 1366 [
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Receptor-Ligand Complex Structure
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PDB
2vs5
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
1.82 Å
Binding residue
(original residue number in PDB)
D225 D227
Binding residue
(residue number reindexed from 1)
D143 D145
Annotation score
1
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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Cellular Component
External links
PDB
RCSB:2vs5
,
PDBe:2vs5
,
PDBj:2vs5
PDBsum
2vs5
PubMed
18651752
UniProt
P14769
|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)
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