Structure of PDB 4gbp Chain A

Receptor sequence

>4gbpA (length=279) Species: 9606 (Homo sapiens)

MVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGL
TVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGR
QLSVLEVGAYKRWQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRD
HVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGA
FFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKV
LSPEYLWDQQLLGWPAVLRKLRFTAVPKN

3D structure

• PDB: 4gbp 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: 2.15 Å

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	GAL	A	R188 D211 M266 G267 A268 W300 D302 E303	R120 D143 M198 G199 A200 W232 D234 E235
BS02	MN	A	D211 D213	D143 D145
BS03	UDP	A	F121 A122 I123 Y126 W181 V184 R188 D211 V212 D213 K346	F53 A54 I55 Y58 W113 V116 R120 D143 V144 D145 K278
BS04	GAL	A	H233 F236 T245 W300 E303	H165 F168 T177 W232 E235

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

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