Structure of PDB 1r80 Chain A

Receptor sequence
>1r80A (length=266) Species: 9606 (Homo sapiens) [Search protein sequence]
MVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQ
NTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRV
TLGTGRQLSVLEVGAYCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLF
GTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGAFFGGSVQEVQR
LTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQL
LGWPAVLRKLRFTAVP
3D structure
PDB1r80 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
Resolution1.65 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) H154 M187 W221 E224 A264
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 AIG A H233 P234 F236 T245 M266 W300 E303 H154 P155 F157 T166 M187 W221 E224
BS02 MN A D211 D213 D132 D134
BS03 UDP A F121 A122 I123 K125 Y126 D211 V212 D213 F59 A60 I61 K63 Y64 D132 V133 D134
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:1r80, PDBe:1r80, PDBj:1r80
PDBsum1r80
PubMed12972418
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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