Structure of PDB 1lzj Chain A Binding Site BS02
Receptor Information
>1lzj Chain A (length=263) Species:
9606
(Homo sapiens) [
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MVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQ
NTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRV
TLGTGRQLSVLEVGERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTL
HPSFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGAFFGGSVQEVQRLTR
ACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQLLGW
PAVLRKLRFTAVP
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1lzj Chain A Residue 406 [
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Receptor-Ligand Complex Structure
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PDB
1lzj
The structural basis for specificity in human ABO(H) blood group biosynthesis.
Resolution
1.32 Å
Binding residue
(original residue number in PDB)
D211 D213
Binding residue
(residue number reindexed from 1)
D129 D131
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H233 M266 W300 E303 A343
Catalytic site (residue number reindexed from 1)
H151 M184 W218 E221 A261
Enzyme Commision number
2.4.1.37
: fucosylgalactoside 3-alpha-galactosyltransferase.
2.4.1.40
: glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase.
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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Cellular Component
External links
PDB
RCSB:1lzj
,
PDBe:1lzj
,
PDBj:1lzj
PDBsum
1lzj
PubMed
12198488
UniProt
P16442
|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)
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