Structure of PDB 4frp Chain A

Receptor sequence
>4frpA (length=274) Species: 9606 (Homo sapiens) [Search protein sequence]
VYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLT
VFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQ
LSVLEVGAYKRWQDVSMRRMEMISCERRFLSEVDYLVCVDVDMEFRDHVG
VEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGAFFG
GSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSP
EYLWDQQLLGWPAVLRKLRFTAVP
3D structure
PDB4frp pH-induced conformational changes in human ABO(H) blood group glycosyltransferases confirm the importance of electrostatic interactions in the formation of the semi-closed state.
ChainA
Resolution2.0 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) H162 M195 W229 E232 A272
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 UDP A F121 A122 I123 Y126 V184 R188 D211 V212 D213 F52 A53 I54 Y57 V115 R119 D140 V141 D142
BS02 MN A D211 D213 D140 D142
BS03 GAL A H233 F236 T245 W300 E303 H162 F165 T174 W229 E232
Gene Ontology
Molecular Function
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4frp, PDBe:4frp, PDBj:4frp
PDBsum4frp
PubMed24265507
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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