Structure of PDB 3ioi Chain A

Receptor sequence
>3ioiA (length=274) Species: 9606 (Homo sapiens) [Search protein sequence]
SLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNT
TIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTL
GTGRQLSVLEVRAMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGV
EILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGDFYYGGAFFGG
SVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPE
YLWDQQLLGWPAVLRKLRFTAVPK
3D structure
PDB3ioi Structural and mechanistic basis for a new mode of glycosyltransferase inhibition.
ChainA
Resolution1.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H233 G266 W300 E303 A343
Catalytic site (residue number reindexed from 1) H161 G194 W228 E231 A271
Enzyme Commision number 2.4.1.37: fucosylgalactoside 3-alpha-galactosyltransferase.
2.4.1.40: glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase.
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 A D211 D213 D139 D141
BS02 1GW A F121 A122 I123 Y126 R188 D211 V212 D213 G267 A268 H301 D302 E303 F57 A58 I59 Y62 R116 D139 V140 D141 G195 A196 H229 D230 E231 MOAD: Ki=0.53uM
PDBbind-CN: -logKd/Ki=6.28,Ki=0.53uM
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:3ioi, PDBe:3ioi, PDBj:3ioi
PDBsum3ioi
PubMed20364127
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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