Structure of PDB 5c4d Chain A

Receptor sequence

>5c4dA (length=279) Species: 9606 (Homo sapiens)

FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVGAYSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFR
DHVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMG
AFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTK
VLSPEYLWDQQLLGWPAVLRKLRFTAVPK

3D structure

• PDB: 5c4d 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 F236 T245 M266 W300 E303 D326 K346	H166 F169 T178 M199 W233 E236 D259 K279
BS03	UPG	A	F121 I123 Y126 R188 D211 V212 D213 M266 G267 A268 D302 E303 K346	F60 I62 Y65 R121 D144 V145 D146 M199 G200 A201 D235 E236 K279

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:5c4d, PDBe:5c4d, PDBj:5c4d
• PDBsum: 5c4d
• PubMed: 26374898
• UniProt: P16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)