Structure of PDB 2rj9 Chain A

Receptor sequence
>2rj9A (length=279) Species: 9606 (Homo sapiens) [Search protein sequence]
FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVGAYKQDVSMRRMEMISRFLSEVDYLVCVDVDMEFRD
HVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGA
FFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKV
LSPEYLWDQQLLGWPAVLRKLRFTAVPKN
3D structure
PDB2rj9 ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes.
ChainA
Resolution1.69 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H233 M266 W300 E303 A343
Catalytic site (residue number reindexed from 1) H165 M198 W232 E235 A275
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 D143 D145
BS02 AD7 A H233 F236 T245 W300 E303 D326 H165 F168 T177 W232 E235 D258
BS03 UDP A F121 A122 I123 Y126 V184 R188 D211 V212 D213 K346 F60 A61 I62 Y65 V121 R125 D143 V144 D145 K278
Gene Ontology
Molecular Function
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2rj9, PDBe:2rj9, PDBj:2rj9
PDBsum2rj9
PubMed18192272
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

[Back to BioLiP]