Structure of PDB 5ltt Chain J Binding Site BS01
Receptor Information
>5ltt Chain J (length=195) Species:
559292
(Saccharomyces cerevisiae S288C) [
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MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEA
GDTVQFAEYIQANIQLYSIREDYELSPQAVSSFVRQELAKSIRSRRPYQV
NVLIGGYDKKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRP
DMTTEEGLDLLKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDDF
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
5ltt Chain J Residue 201 [
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Receptor-Ligand Complex Structure
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PDB
5ltt
A humanized yeast proteasome identifies unique binding modes of inhibitors for the immunosubunit beta 5i.
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
Q118 D120
Binding residue
(residue number reindexed from 1)
Q118 D120
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
S18 A20 K34 G48 Y135
Catalytic site (residue number reindexed from 1)
S18 A20 K34 G48 Y135
Enzyme Commision number
3.4.25.1
: proteasome endopeptidase complex.
Gene Ontology
Molecular Function
GO:0005515
protein binding
GO:0061133
endopeptidase activator activity
Biological Process
GO:0010498
proteasomal protein catabolic process
GO:0010499
proteasomal ubiquitin-independent protein catabolic process
GO:0043161
proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0051603
proteolysis involved in protein catabolic process
Cellular Component
GO:0000502
proteasome complex
GO:0005634
nucleus
GO:0005737
cytoplasm
GO:0005789
endoplasmic reticulum membrane
GO:0005829
cytosol
GO:0005839
proteasome core complex
GO:0019774
proteasome core complex, beta-subunit complex
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:5ltt
,
PDBe:5ltt
,
PDBj:5ltt
PDBsum
5ltt
PubMed
27789522
UniProt
P22141
|PSB4_YEAST Proteasome subunit beta type-4 (Gene Name=PRE1)
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