Structure of PDB 5c36 Chain A

Receptor sequence

>5c36A (length=288) Species: 9606 (Homo sapiens)

AIGEFMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNE
QFRLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPA
AVPRVTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYL
VCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIP
KDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLN
KYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVP

3D structure

• PDB: 5c36 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: 1.55 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H233 L266 W300 E303 A343
• Catalytic site (residue number reindexed from 1): H176 L209 W243 E246 A286
• 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	D154 D156
BS02	DA8	A	H233 F236 T245 W300 E303 D326	H176 F179 T188 W243 E246 D269
BS03	UDP	A	F121 A122 I123 Y126 V184 R188 D211 V212 D213	F64 A65 I66 Y69 V127 R131 D154 V155 D156

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:5c36, PDBe:5c36, PDBj:5c36
• PDBsum: 5c36
• PubMed: 26374898
• UniProt: P16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)