Structure of PDB 5c1l Chain A

Receptor sequence

>5c1lA (length=279) Species: 9606 (Homo sapiens)

FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVGAVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFR
DHVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMG
AFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTK
VLSPEYLWDQQLLGWPAVLRKLRFTAVPK

3D structure

• PDB: 5c1l 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): H166 M199 W233 E236 A276
• 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	D144 D146
BS02	DA8	A	H233 S235 F236 T245 W300 E303 D326	H166 S168 F169 T178 W233 E236 D259
BS03	GDU	A	F121 I123 Y126 D211 V212 D213 W300 H301 E303	F60 I62 Y65 D144 V145 D146 W233 H234 E236

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:5c1l, PDBe:5c1l, PDBj:5c1l
• PDBsum: 5c1l
• PubMed: 26374898
• UniProt: P16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)