Structure of PDB 8eqx Chain B

Receptor sequence
>8eqxB (length=767) Species: 759272 (Thermochaetoides thermophila DSM 1495) [Search protein sequence]
ESILHSEIGRLNNQSLLWGPYRPNIYFGTRPRIGKSLMTGLMWGKIESYT
DFQHTVRYTCEQNEGMKGYGWDEYDPRRGGIQSIHDIQNGLDITTSFVKI
PGGAHGGSWAARIKGTLNDDAPKDQKTIVVFYVSQEGENSELEAVPSENE
FGYEGDVILKGRSEALGNYKLVVTKGKGVIPQSDHDLSRLRGPGQTVVQS
LTYPDEVLWQAKPILFQQLKAGIDWLVENKYDVADPPPPWQVYLLANKPG
SGNVHIVQKVFEGDFEFDILFSSESAGKEVTSKDLEREVKQATEVFGERF
ARVFDLKAPFQGDNYKKFGKSMFSNLIGGIGYFYGHSLVDRSYAPEYDEE
NEGFWEDAAEARARHQEALEGPYELFTSIPSRPFFPRGFLWDEGFHLLPI
ADWDIDLALEIIKSWYNLMDEDGWIAREQILGAEARSKVPKEFQTQYPHY
ANPPTLFLVLDNFVERLRKNNATLSTASVDNPEVGLEYLRRLYPLLRRQF
DWFRKTQAGDIKSYDREAYSTKEAYRWRGRTVSHCLTSGLDDYPRPQPPH
PGELHVDLMSWVGVMVKSLISIGSLLGATEDVEFYTKVLDAIEHNLDDLH
WSEKEGCYCDATIDEFEEHKLVCHKGYISLFPFLTGLLKPDSPKLGKLLA
LIGDESELWSPYGLRSLSKKDEFYGTAENYWRSPVWININYLAIVQLYNI
ATQDGPYKETARDLYTRLRKNIVETVYRNWEETGFAWEQYNPETGKGQRT
QHFTGWTSLVVKIMSGH
3D structure
PDB8eqx Structure-Based Design of Potent Iminosugar Inhibitors of Endoplasmic Reticulum alpha-Glucosidase I with Anti-SARS-CoV-2 Activity.
ChainB
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.106: mannosyl-oligosaccharide glucosidase.
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 WT5 B F416 F417 F421 W423 D424 G584 D586 F384 F385 F389 W391 D392 G539 D541
Gene Ontology
Molecular Function
GO:0004573 Glc3Man9GlcNAc2 oligosaccharide glucosidase activity
GO:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006487 protein N-linked glycosylation
GO:0009311 oligosaccharide metabolic process
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:8eqx, PDBe:8eqx, PDBj:8eqx
PDBsum8eqx
PubMed36762932
UniProtG0SFD1

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