Structure of PDB 2vfz Chain A

Receptor sequence
>2vfzA (length=278) Species: 9913 (Bos taurus) [Search protein sequence]
KLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGL
TVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPL
RSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQ
DKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHA
AIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHLNKYFLLNKPTK
ILSPEYCWDYHIGLPADIKLVKMSWQTK
3D structure
PDB2vfz Conformational Changes Induced by Binding Udp-2F-Galactose to Alpha-1,3 Galactosyltransferase-Implications for Catalysis
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W314
Catalytic site (residue number reindexed from 1) W233
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 UPF A F134 V136 Y139 I198 S199 R202 D225 V226 D227 H280 A281 A282 D316 E317 K359 F53 V55 Y58 I117 S118 R121 D144 V145 D146 H199 A200 A201 D235 E236 K278 MOAD: Ki=245uM
PDBbind-CN: -logKd/Ki=3.61,Ki=245uM
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:2vfz, PDBe:2vfz, PDBj:2vfz
PDBsum2vfz
PubMed17493636
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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