Structure of PDB 5c3b Chain A

Receptor sequence

>5c3bA (length=277) Species: 9606 (Homo sapiens)

FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVRSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDH
VGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGGF
FGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVL
SPEYLWDQQLLGWPAVLRKLRFTAVPK

3D structure

• PDB: 5c3b High Resolution Structures of the Human ABO(H) Blood Group Enzymes in Complex with Donor Analogs Reveal That the Enzymes Utilize Multiple Donor Conformations to Bind Substrates in a Stepwise Manner.
• Chain: A
• Resolution: 1.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H233 M266 W300 E303 A343
• Catalytic site (residue number reindexed from 1): H164 M197 W231 E234 A274
• 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	D142 D144
BS02	DA8	A	H233 S235 F236 T245 W300 E303 D326 L329 K346	H164 S166 F167 T176 W231 E234 D257 L260 K277
BS03	URM	A	F121 A122 I123 Y126 D211 V212 D213 W300 H301 E303	F60 A61 I62 Y65 D142 V143 D144 W231 H232 E234

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:5c3b, PDBe:5c3b, PDBj:5c3b
• PDBsum: 5c3b
• PubMed: 26374898
• UniProt: P16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)