Structure of PDB 1g8o Chain A

Receptor sequence
>1g8oA (length=287) Species: 9913 (Bos taurus) [Search protein sequence]
SKLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVG
LTVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGP
LRSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVF
QDKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYH
AAIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHLNKYFLLNKPT
KILSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVRNN
3D structure
PDB1g8o Bovine alpha1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases.
ChainA
Resolution2.3 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 R365
Catalytic site (residue number reindexed from 1) Q167 H200 W234 E237 W276 R285
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 MN A D225 D227 N362 D145 D147 N282
BS02 U5P A F134 A135 V136 R138 Y139 I198 R202 D225 V226 D227 E360 N362 F54 A55 V56 R58 Y59 I118 R122 D145 V146 D147 E280 N282
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:1g8o, PDBe:1g8o, PDBj:1g8o
PDBsum1g8o
PubMed11179209
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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