Structure of PDB 1g93 Chain A Binding Site BS02
Receptor Information
>1g93 Chain A (length=277) Species:
9913
(Bos taurus) [
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KLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGL
TVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPL
RSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQ
DKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHA
AIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHLNKYFLLNKPTK
ILSPEYCWDYHIGLPADIKLVKMSWQT
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
1g93 Chain A Residue 1000 [
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Receptor-Ligand Complex Structure
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PDB
1g93
Bovine alpha1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases.
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
D225 D227
Binding residue
(residue number reindexed from 1)
D144 D146
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
Q247 H280 W314 E317 W356
Catalytic site (residue number reindexed from 1)
Q166 H199 W233 E236 W275
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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Cellular Component
External links
PDB
RCSB:1g93
,
PDBe:1g93
,
PDBj:1g93
PDBsum
1g93
PubMed
11179209
UniProt
P14769
|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)
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