Structure of PDB 4frb Chain A

Receptor sequence

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

FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVRAYKQDVSMRRMEMISCERRFLSEVDYLVCVDVDME
FRDHVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYY
MGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKP
TKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKN

3D structure

• PDB: 4frb 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: 1.54 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H233 M266 W300 E303 A343
• Catalytic site (residue number reindexed from 1): H168 M201 W235 E238 A278
• 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 I123 Y126 V184 R188 D211 V212 D213 K346	F60 I62 Y65 V121 R125 D146 V147 D148 K281
BS02	GAL	A	H233 F236 T245 W300 E303	H168 F171 T180 W235 E238
BS03	MN	A	D211 D213	D146 D148

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

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