Structure of PDB 5c4e Chain A

Receptor sequence

>5c4eA (length=290) Species: 9606 (Homo sapiens)

FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVGAYKRDVSMRRMEMISDFCERRFLSEVDYLVCVDVD
MEFRDHVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDF
YYMGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRH
KPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRN

3D structure

• PDB: 5c4e 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: 1.55 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H233 M266 W300 E303 A343 R352
• Catalytic site (residue number reindexed from 1): H170 M203 W237 E240 A280 R289
• 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	UDP	A	F121 A122 I123 Y126 D211 V212 D213 K346 R352	F60 A61 I62 Y65 D148 V149 D150 K283 R289
BS03	4YA	A	H233 F236 T245 M266 W300 E303 D326 H348	H170 F173 T182 M203 W237 E240 D263 H285

Gene Ontology

Molecular Function

• GO:0016758 hexosyltransferase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:5c4e, PDBe:5c4e, PDBj:5c4e
• PDBsum: 5c4e
• PubMed: 26374898
• UniProt: P16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)