Structure of PDB 3v0n Chain B

Receptor sequence
>3v0nB (length=288) Species: 9606 (Homo sapiens) [Search protein sequence]
AIGEFMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNE
QFRLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPA
AVPRVTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYL
VCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIP
KDEGDFYYGGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLN
KYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVP
3D structure
PDB3v0n Base-modified donor analogues reveal novel dynamic features of a glycosyltransferase.
ChainB
Resolution1.75 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) H176 G209 W243 E246 A286
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 B D211 D213 D154 D156
BS02 3GW B F121 I123 Y126 W181 D211 V212 D213 H233 A268 E303 F64 I66 Y69 W124 D154 V155 D156 H176 A211 E246
BS03 4GW B F121 I123 Y126 W181 D211 V212 D213 F64 I66 Y69 W124 D154 V155 D156
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:3v0n, PDBe:3v0n, PDBj:3v0n
PDBsum3v0n
PubMed23836908
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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