Structure of PDB 5c4b Chain A

Receptor sequence

>5c4bA (length=288) Species: 9606 (Homo sapiens)

AIGEFMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNE
QFRLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPA
AVPRVTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYL
VCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIP
KDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLN
KYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVP

3D structure

• PDB: 5c4b 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: 1.54 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	DA8	A	H233 F236 T245 W300 E303 D326	H176 F179 T188 W243 E246 D269
BS02	UPG	A	F121 A122 I123 Y126 W181 V184 S185 R188 D211 V212 D213 G267 G268 D302 E303	F64 A65 I66 Y69 W124 V127 S128 R131 D154 V155 D156 G210 G211 D245 E246

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:5c4b, PDBe:5c4b, PDBj:5c4b
• PDBsum: 5c4b
• PubMed: 26374898
• UniProt: P16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)