Structure of PDB 3i0l Chain A

Receptor sequence
>3i0lA (length=272) Species: 9606 (Homo sapiens) [Search protein sequence]
MVYPQPKVLTPSRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGL
TVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGR
QLSVLEVGDVSMRRMEMISDFSERRFLSEVDYLVSVDVDMEFRDHVGVEI
LTPLFGTLHPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGAFFGGSV
QEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYL
WDQQLLGWPAVLRKLRFTAVPK
3D structure
PDB3i0l Cysteine-to-serine mutants dramatically reorder the active site of human ABO(H) blood group B glycosyltransferase without affecting activity: structural insights into cooperative substrate binding
ChainA
Resolution1.6 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) H159 M192 W226 E229 A269
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 P72 S80 G98 T99 F100 N101 P4 S12 G30 T31 F32 N33
BS02 UDP A F121 A122 I123 Y126 D211 V212 D213 F53 A54 I55 Y58 D137 V138 D139
BS03 GAL A G267 W300 H301 D302 E303 G193 W226 H227 D228 E229
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:3i0l, PDBe:3i0l, PDBj:3i0l
PDBsum3i0l
PubMed20655926
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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