Structure of PDB 1r82 Chain A

Receptor sequence
>1r82A (length=263) Species: 9606 (Homo sapiens) [Search protein sequence]
MVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQ
NTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRV
TLGTGRQLSVLEVCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTL
HPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGAFFGGSVQEVQRLTR
ACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQLLGW
PAVLRKLRFTAVP
3D structure
PDB1r82 The influence of an intramolecular hydrogen bond in differential recognition of inhibitory acceptor analogs by human ABO(H) blood group A and B glycosyltransferases
ChainA
Resolution1.55 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 AOG A H233 P234 S235 F236 T245 W300 E303 W325 D326 H151 P152 S153 F154 T163 W218 E221 W243 D244
BS02 GDU A F121 A122 Y126 D211 D213 F59 A60 Y64 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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Cellular Component
External links
PDB RCSB:1r82, PDBe:1r82, PDBj:1r82
PDBsum1r82
PubMed12972418
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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