Structure of PDB 2rj5 Chain A

Receptor sequence
>2rj5A (length=282) Species: 9606 (Homo sapiens) [Search protein sequence]
FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISCERRFLSEVDYLVCVDVD
MEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGDF
YYMGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRH
KPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVP
3D structure
PDB2rj5 ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes.
ChainA
Resolution1.45 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) H170 M203 W237 E240 A280
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 A D211 D213 D148 D150
BS02 UDP A F121 A122 I123 Y126 V184 R188 D211 V212 D213 F60 A61 I62 Y65 V123 R127 D148 V149 D150
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:2rj5, PDBe:2rj5, PDBj:2rj5
PDBsum2rj5
PubMed18192272
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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