Structure of PDB 5c3a Chain A

Receptor sequence
>5c3aA (length=282) Species: 9606 (Homo sapiens) [Search protein sequence]
FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVRAYQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDM
EFRDHVGVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFY
YMGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHK
PTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPK
3D structure
PDB5c3a 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.
ChainA
Resolution1.33 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H233 M266 W300 E303 A343
Catalytic site (residue number reindexed from 1) H169 M202 W236 E239 A279
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 D147 D149
BS02 URM A F121 I123 Y126 V184 D211 V212 D213 H233 W300 E303 K346 F60 I62 Y65 V120 D147 V148 D149 H169 W236 E239 K282
Gene Ontology
Molecular Function
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane

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Cellular Component
External links
PDB RCSB:5c3a, PDBe:5c3a, PDBj:5c3a
PDBsum5c3a
PubMed26374898
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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