Structure of PDB 4no8 Chain I Binding Site BS01

Receptor Information
>4no8 Chain I (length=204) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFL
GITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERRFG
PYFVGPVVAGINSKSGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCE
SLYEPNLEPEDLFETISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLK
MRQD
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain4no8 Chain I Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4no8 Systematic Comparison of Peptidic Proteasome Inhibitors Highlights the alpha-Ketoamide Electrophile as an Auspicious Reversible Lead Motif.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		D177 A178
Binding residue
(residue number reindexed from 1)		D177 A178
Annotation score4
Enzymatic activity
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: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:0005829 cytosol
GO:0005839 proteasome core complex
GO:0019774 proteasome core complex, beta-subunit complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4no8, PDBe:4no8, PDBj:4no8
PDBsum4no8
PubMed24403024
UniProtP25451|PSB3_YEAST Proteasome subunit beta type-3 (Gene Name=PUP3)

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