Structure of PDB 1g93 Chain A

Receptor sequence
>1g93A (length=277) Species: 9913 (Bos taurus) [Search protein sequence]
KLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGL
TVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPL
RSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQ
DKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHA
AIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHLNKYFLLNKPTK
ILSPEYCWDYHIGLPADIKLVKMSWQT
3D structure
PDB1g93 Bovine alpha1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GAL A Q247 W250 Y278 H280 W314 E317 Q166 W169 Y197 H199 W233 E236
BS02 MN A D225 D227 D144 D146
BS03 UPG A V136 Y139 W195 I198 R202 D225 V226 A281 A282 H315 D316 E317 V55 Y58 W114 I117 R121 D144 V145 A200 A201 H234 D235 E236
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
PDBsum1g93
PubMed11179209
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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