Structure of PDB 2rj1 Chain A

Receptor sequence
>2rj1A (length=291) Species: 9606 (Homo sapiens) [Search protein sequence]
FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISCERRFLSEVDYLVCVDVD
MEFRDHVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDF
YYMGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRH
KPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP
3D structure
PDB2rj1 ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes.
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 R352
Catalytic site (residue number reindexed from 1) H170 M203 W237 E240 A280 R289
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 BHE A H233 F236 T245 W300 E303 D326 L329 H348 H170 F173 T182 W237 E240 D263 L266 H285
BS03 UDP A F121 I123 Y126 V184 R188 D211 V212 D213 K346 R352 F60 I62 Y65 V123 R127 D148 V149 D150 K283 R289
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:2rj1, PDBe:2rj1, PDBj:2rj1
PDBsum2rj1
PubMed18192272
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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