Structure of PDB 6sni Chain X

Receptor sequence
>6sniX (length=479) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
PEYIIFVCAVILRCTIGLGPYSGKGSPPLYGDFEAQRHWMEITQHLPLSK
WYWYDLQYWGLDYPPLTAFHSYLLGLIGSFFNPSWFALEKSRGFESPDNG
LKTYMRSTVIISDILFYFPAVIYFTKWLGRYRNQSPIGQSIAASAILFQP
SLMLIDHGHFQYNSVMLGLTAYAINNLLDEYYAMAAVCFVLSICFKQMAL
YYAPIFFAYLLSRSLLFPKFNIARLTVIAFATLATFAIIFAPLYFLGGGL
KNIHQCIHRIFPFARGIFEDKVANFWCVTNVFVKYKERFTIQQLQLYSLI
ATVIGFLPAMIMTLLHPKKHLLPYVLIACSMSFFLFSFQVHEKTILIPLL
PITLLYSSTDWNVLSLVSWINNVALFTLWPLLKKDGLHLQYAVSFLLSNW
LIGNFSLLPYNVVWKSFIIGTYIAMGFYHFLDQFVAPPSKYPDLWVLLNC
AVGFICFSIFWLWSYYKIFTSGSKSMKDL
3D structure
PDB6sni Structure and mechanism of the ER-based glucosyltransferase ALG6.
ChainX
Resolution3.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.267: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase.
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 Y01 X P241 T339 F370 P204 T302 F333
BS02 Y01 X I230 F277 I193 F240
BS03 Y01 X A301 Q332 A264 Q295
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
GO:0016758 hexosyltransferase activity
GO:0042281 dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity
Biological Process
GO:0006486 protein glycosylation
GO:0006487 protein N-linked glycosylation
GO:0006488 dolichol-linked oligosaccharide biosynthetic process
GO:0009060 aerobic respiration
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
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:6sni, PDBe:6sni, PDBj:6sni
PDBsum6sni
PubMed32103179
UniProtQ12001|ALG6_YEAST Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase (Gene Name=ALG6)

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