Structure of PDB 8v9q Chain B Binding Site BS01
Receptor Information
>8v9q Chain B (length=449) Species:
10090
(Mus musculus) [
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GPGEMPVVIPKEKMKEMFKINQASEMIALNRSLPDVRLEGCKTKVYPDNL
PTTSVVIFHNESTLRTVHSVINRSPRHMIEEIVDASERDFLKRPSYVKKL
KVPVVIREQRSGLIRARLSRGQVTFLDAHCETAGWLEPLLARIKHDRRTV
CPIIDVISDDTFEYMAGSDMTYGFNWKLNFRWYPVPQREMDRRKGDRTLP
VRTPTMALFSIDRDYFQEIGTYDAGMDIWGGENLEISFRIWQCGGTLEIV
TCSHVGHVFRKATPYQIINKNNRRLAEVWMDEFKNFFYIISVTKVDYGDI
SSRLGLRRKLQCKPFSWYLENIYPDSQIPRHYFSLGEIRNVETNQCLDNM
AKENEKVGIFNCHGMGNQVFSYTANKEIRTDDLCLDVSKLNPVTMLKCHH
LKNQLWEDPVKLTLQHVNSNQCLDKAQVPSIRDCTGSRSQQWLLRNVTL
Ligand information
>8v9q Chain F (length=15) Species:
9606
(Homo sapiens) [
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GTTPSPVPTSTTSAP
Receptor-Ligand Complex Structure
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PDB
8v9q
An unusual dual sugar-binding lectin domain controls the substrate specificity of a mucin-type O-glycosyltransferase.
Resolution
2.29 Å
Binding residue
(original residue number in PDB)
V240 F265 R266 W267 F346 R347 E450 N503
Binding residue
(residue number reindexed from 1)
V156 F180 R181 W182 F259 R260 E353 N403
Enzymatic activity
Enzyme Commision number
2.4.1.41
: polypeptide N-acetylgalactosaminyltransferase.
Gene Ontology
Molecular Function
GO:0004653
polypeptide N-acetylgalactosaminyltransferase activity
GO:0016757
glycosyltransferase activity
GO:0030145
manganese ion binding
GO:0030246
carbohydrate binding
GO:0046872
metal ion binding
Biological Process
GO:0006486
protein glycosylation
GO:0006493
protein O-linked glycosylation
GO:0018242
protein O-linked glycosylation via serine
GO:0018243
protein O-linked glycosylation via threonine
Cellular Component
GO:0005576
extracellular region
GO:0005794
Golgi apparatus
GO:0016020
membrane
GO:0032580
Golgi cisterna membrane
GO:0048471
perinuclear region of cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:8v9q
,
PDBe:8v9q
,
PDBj:8v9q
PDBsum
8v9q
PubMed
38416819
UniProt
O08912
|GALT1_MOUSE Polypeptide N-acetylgalactosaminyltransferase 1 (Gene Name=Galnt1)
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