Structure of PDB 5c48 Chain A

Receptor sequence

>5c48A (length=282) Species: 9606 (Homo sapiens)

GEFMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQF
RLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAV
PRVTLGTGRQLSVLEVGAYVSMRRMEMISDFCERRFLSEVDYLVCVDVDM
EFRDHVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFY
YMGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHK
PTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPK

3D structure

• PDB: 5c48 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: 1.46 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H233 M266 W300 E303 A343
• Catalytic site (residue number reindexed from 1): H169 M202 W236 E239 A279
• 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	D147 D149
BS02	DA8	A	H233 F236 T245 M266 W300 E303 D326 K346	H169 F172 T181 M202 W236 E239 D262 K282
BS03	URM	A	F121 A122 I123 K124 Y126 D211 V212 D213 W300 H301 E303	F62 A63 I64 K65 Y67 D147 V148 D149 W236 H237 E239

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:5c48, PDBe:5c48, PDBj:5c48
• PDBsum: 5c48
• PubMed: 26374898
• UniProt: P16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)