Structure of PDB 5c8r Chain A

Receptor sequence

>5c8rA (length=278) Species: 9606 (Homo sapiens)

GEFMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQF
RLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAV
PRVTLGTGRQLSVLEVRMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRD
HVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGG
FFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKV
LSPEYLWDQQLLGWPAVLRKLRFTAVPK

3D structure

• PDB: 5c8r 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: 1.45 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	MN	A	D211 D213	D143 D145
BS02	DA8	A	H233 F236 T245 W300 E303 D326 K346	H165 F168 T177 W232 E235 D258 K278
BS03	UPG	A	F121 I123 Y126 R188 D211 V212 D213 G267 G268 W300 D302	F62 I64 Y67 R120 D143 V144 D145 G199 G200 W232 D234

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:5c8r, PDBe:5c8r, PDBj:5c8r
• PDBsum: 5c8r
• PubMed: 26374898
• UniProt: P16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)