Structure of PDB 4frd Chain A

Receptor sequence

>4frdA (length=282) Species: 9606 (Homo sapiens)

FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISCERRFLSEVDYLVCVDVD
MEFRDHVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDF
YYMGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRH
KPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVP

3D structure

• PDB: 4frd 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.
• Chain: A
• Resolution: 1.55 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H233 M266 W300 E303 A343
• Catalytic site (residue number reindexed from 1): H170 M203 W237 E240 A280
• 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 V184 R188 D211 V212 D213	F60 A61 I62 Y65 V123 R127 D148 V149 D150
BS02	GAL	A	H233 F236 T245 W300 E303	H170 F173 T182 W237 E240
BS03	MN	A	D211 D213	D148 D150

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:4frd, PDBe:4frd, PDBj:4frd
• PDBsum: 4frd
• PubMed: 24265507
• UniProt: P16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)