Structure of PDB 3v0q Chain B

Receptor sequence
>3v0qB (length=297) Species: 9606 (Homo sapiens) [Search protein sequence]
AIGEFMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNE
QFRLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPA
AVPRVTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYL
VCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIP
KDEGDFYYGGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLN
KYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP
3D structure
PDB3v0q Base-modified Donor Analogues Reveal Novel Dynamic Features of a Glycosyltransferase.
ChainB
Resolution1.8 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 R352
Catalytic site (residue number reindexed from 1) H176 G209 W243 E246 A286 R295
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 UDP B F121 I123 Y126 V184 R188 D211 V212 D213 K346 R352 F64 I66 Y69 V127 R131 D154 V155 D156 K289 R295
BS03 BHE B H233 F236 T245 W300 E303 D326 L329 H348 H176 F179 T188 W243 E246 D269 L272 H291
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:3v0q, PDBe:3v0q, PDBj:3v0q
PDBsum3v0q
PubMed23836908
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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