Structure of PDB 2rj4 Chain A

Receptor sequence
>2rj4A (length=290) Species: 9606 (Homo sapiens) [Search protein sequence]
FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISFCERRFLSEVDYLVCVDV
DMEFRDHVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGD
FYYMGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLR
HKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVR
3D structure
PDB2rj4 ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes.
ChainA
Resolution1.47 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) H171 M204 W238 E241 A281 R290
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 D149 D151
BS02 UDP A F121 A122 I123 Y126 V184 R188 D211 V212 D213 K346 H348 R352 F60 A61 I62 Y65 V123 R127 D149 V150 D151 K284 H286 R290
BS03 AD7 A H233 F236 T245 W300 E303 D326 L329 H171 F174 T183 W238 E241 D264 L267
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:2rj4, PDBe:2rj4, PDBj:2rj4
PDBsum2rj4
PubMed18192272
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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