Structure of PDB 4frq Chain A

Receptor sequence
>4frqA (length=277) Species: 9606 (Homo sapiens) [Search protein sequence]
VYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLT
VFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQ
LSVLEVGAYKRWQDVSMRRMEMISACERRFLSEVDYLVCVDVDMEFRDHV
GVEILTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGAFF
GGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLS
PEYLWDQQLLGWPAVLRKLRFTAVPKN
3D structure
PDB4frq 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
Resolution2.35 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) H163 M196 W230 E233 A273
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 I123 Y126 V184 R188 D211 V212 D213 K346 F52 I54 Y57 V115 R119 D141 V142 D143 K276
BS02 MN A D211 D213 D141 D143
BS03 GAL A H233 F236 T245 W300 E303 H163 F166 T175 W230 E233
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:4frq, PDBe:4frq, PDBj:4frq
PDBsum4frq
PubMed24265507
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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