Structure of PDB 2vfz Chain B

Receptor sequence
>2vfzB (length=281) Species: 9913 (Bos taurus) [Search protein sequence]
LKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGLT
VFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPLR
SFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQD
KFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHAA
IFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHLNKYFLLNKPTKI
LSPEYCWDYHIGLPADIKLVKMSWQTKEYNV
3D structure
PDB2vfz Conformational Changes Induced by Binding Udp-2F-Galactose to Alpha-1,3 Galactosyltransferase-Implications for Catalysis
ChainB
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) Q1247 H1280 W1314 E1317 W1356
Catalytic site (residue number reindexed from 1) Q165 H198 W232 E235 W274
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 B F1134 A1135 V1136 Y1139 W1195 I1198 S1199 R1202 D1225 V1226 D1227 H1280 A1281 A1282 H1315 D1316 E1317 K1359 F52 A53 V54 Y57 W113 I116 S117 R120 D143 V144 D145 H198 A199 A200 H233 D234 E235 K277 MOAD: Ki=245uM
BS02 MN B D1225 D1227 K1359 D143 D145 K277
Gene Ontology
Molecular Function
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane

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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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