Structure of PDB 4fre Chain A

Receptor sequence
>4freA (length=264) Species: 9606 (Homo sapiens) [Search protein sequence]
YPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTV
FAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQL
SVLEVGRRMEMISGCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGT
LHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGAFFGGSVQEVQRLT
RACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQLLG
WPAVLRKLRFTAVP
3D structure
PDB4fre pH-induced conformational changes in human ABO(H) blood group glycosyltransferases confirm the importance of electrostatic interactions in the formation of the semi-closed state.
ChainA
Resolution1.85 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) H152 M185 W219 E222 A262
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 UDP A F121 A122 I123 Y126 D211 V212 D213 F51 A52 I53 Y56 D130 V131 D132
BS02 GAL A H233 F236 T245 W300 E303 H152 F155 T164 W219 E222
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:4fre, PDBe:4fre, PDBj:4fre
PDBsum4fre
PubMed24265507
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

[Back to BioLiP]