Structure of PDB 2vs5 Chain B

Receptor sequence
>2vs5B (length=277) Species: 9913 (Bos taurus) [Search protein sequence]
KLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGL
TVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPL
RSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQ
DKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHA
AIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDQSHLNKYFLLNKPTK
ILSPEYCWDYHIGLPADIKLVKMSWQT
3D structure
PDB2vs5 Structural Basis of Udp-Galactose Binding by Alpha- 1,3-Galactosyltransferase (Alpha3Gt): Role of Negative Charge on Aspartic Acid 316 in Structure and Activity.
ChainB
Resolution1.82 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 Q317 W356
Catalytic site (residue number reindexed from 1) Q166 H199 W233 Q236 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 MN B D225 D227 D144 D146
BS02 GDU B F134 A135 V136 Y139 W195 I198 S199 R202 D225 V226 D227 H280 A281 A282 H315 D316 Q317 F53 A54 V55 Y58 W114 I117 S118 R121 D144 V145 D146 H199 A200 A201 H234 D235 Q236
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:2vs5, PDBe:2vs5, PDBj:2vs5
PDBsum2vs5
PubMed18651752
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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