Structure of PDB 1gww Chain A

Receptor sequence
>1gwwA (length=287) Species: 9913 (Bos taurus) [Search protein sequence]
KLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGL
TVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPL
RSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQ
DKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHA
AIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHLNKYFLLNKPTK
ILSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVRNNV
3D structure
PDB1gww Structural Basis of Ordered Binding of Donor and Acceptor Substrates to the Retaining Glycosyltransferase, Alpha -1,3 Galactosyltransferase
ChainA
Resolution1.8 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) Q166 H199 W233 E236 W275 R284
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 UDP A F134 A135 V136 Y139 I198 R202 D225 V226 D227 K359 Y361 R365 F53 A54 V55 Y58 I117 R121 D144 V145 D146 K278 Y280 R284 PDBbind-CN: -logKd/Ki=3.59,Kd=0.258mM
BS02 MN A D225 D227 D144 D146
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:1gww, PDBe:1gww, PDBj:1gww
PDBsum1gww
PubMed12011052
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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