Structure of PDB 2a8u Chain A

Receptor sequence
>2a8uA (length=263) Species: 9606 (Homo sapiens) [Search protein sequence]
FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTL
HPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGAFFGGSVQEVQRLTR
ACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQLLGW
PAVLRKLRFTAVP
3D structure
PDB2a8u Differential Recognition of the Type I and II H Antigen Acceptors by the Human ABO(H) Blood Group A and B Glycosyltransferases.
ChainA
Resolution1.69 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 M266 W300 E303 A343
Catalytic site (residue number reindexed from 1) H151 M184 W218 E221 A261
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 GAL A H233 F236 T245 W300 E303 H151 F154 T163 W218 E221
BS02 UDP A F121 A122 I123 Y126 D211 V212 D213 F60 A61 I62 Y65 D129 V130 D131
BS03 MN A D211 D213 D129 D131
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:2a8u, PDBe:2a8u, PDBj:2a8u
PDBsum2a8u
PubMed16326711
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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