Structure of PDB 2rj7 Chain A

Receptor sequence
>2rj7A (length=292) Species: 9606 (Homo sapiens) [Search protein sequence]
FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISFCERRFLSEVDYLVCVDV
DMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGD
FYYMGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLR
HKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP
3D structure
PDB2rj7 ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes.
ChainA
Resolution1.7 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 GDU A F121 A122 I123 Y126 V184 S185 R188 D211 V212 D213 G267 A268 H301 D302 K346 R352 F60 A61 I62 Y65 V123 S124 R127 D149 V150 D151 G205 A206 H239 D240 K284 R290
BS02 MN A D211 D213 D149 D151
BS03 DA8 A H233 F236 T245 W300 E303 D326 H348 H171 F174 T183 W238 E241 D264 H286
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:2rj7, PDBe:2rj7, PDBj:2rj7
PDBsum2rj7
PubMed18192272
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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