Structure of PDB 1o7o Chain B

Receptor sequence
>1o7oB (length=287) Species: 9913 (Bos taurus) [Search protein sequence]
KLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGL
TVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPL
RSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQ
DKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHA
AIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDQSHLNKYFLLNKPTK
ILSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVRNNV
3D structure
PDB1o7o Roles of individual enzyme-substrate interactions by alpha-1,3-galactosyltransferase in catalysis and specificity.
ChainB
Resolution1.97 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 Q1317 W1356 R1365
Catalytic site (residue number reindexed from 1) Q166 H199 W233 Q236 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 BGC B W1249 W1250 W168 W169
BS02 GAL B Q1247 T1259 W1314 Q1317 W1356 Q166 T178 W233 Q236 W275
BS03 MN B D1225 D1227 D144 D146
BS04 UDP B F1134 A1135 V1136 Y1139 I1198 R1202 D1225 V1226 D1227 K1359 Y1361 R1365 F53 A54 V55 Y58 I117 R121 D144 V145 D146 K278 Y280 R284 MOAD: Kd=0.032mM
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:1o7o, PDBe:1o7o, PDBj:1o7o
PDBsum1o7o
PubMed14621997
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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