Structure of PDB 5c4f Chain A

Receptor sequence

>5c4fA (length=283) Species: 9606 (Homo sapiens)

AIGEFMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNE
QFRLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPA
AVPRVTLGTGRQLSVLEVRAYSMRRMEMISDFCERRFLSEVDYLVCVDVD
MEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGDF
YYMGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRH
KPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPK

3D structure

• PDB: 5c4f 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: 1.41 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H233 M266 W300 E303 A343
• Catalytic site (residue number reindexed from 1): H170 M203 W237 E240 A280
• 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	D148 D150
BS02	DA8	A	H233 F236 T245 M266 W300 E303 D326	H170 F173 T182 M203 W237 E240 D263
BS03	UPG	A	F121 I123 Y126 S185 R188 D211 V212 D213 M266 G267 A268 D302 E303	F64 I66 Y69 S122 R125 D148 V149 D150 M203 G204 A205 D239 E240

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:5c4f, PDBe:5c4f, PDBj:5c4f
• PDBsum: 5c4f
• PubMed: 26374898
• UniProt: P16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)