Structure of PDB 1o7q Chain A

Receptor sequence
>1o7qA (length=287) Species: 9913 (Bos taurus) [Search protein sequence]
KLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGL
TVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPL
RSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQ
DKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHA
AIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHLNKYFLLNKPTK
ILSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVRNNV
3D structure
PDB1o7q Roles of Individual Enzyme-Substrate Interactions by Alpha-1,3-Galactosyltransferase in Catalysis and Specificity.
ChainA
Resolution1.3 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 GAL A Q247 T259 W314 E317 W356 Q166 T178 W233 E236 W275
BS02 MN A D225 D227 D144 D146
BS03 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 MOAD: Kd=0.032mM
BS04 UDP A R194 K306 R113 K225 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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Molecular Function
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Cellular Component
External links
PDB RCSB:1o7q, PDBe:1o7q, PDBj:1o7q
PDBsum1o7q
PubMed14621997
UniProtP14769|GGTA1_BOVIN N-acetyllactosaminide alpha-1,3-galactosyltransferase (Gene Name=GGTA1)

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