Structure of PDB 4inu Chain W Binding Site BS01

Receptor Information
>4inu Chain W (length=204) Species: 4932 (Saccharomyces cerevisiae) [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 ID1G6
InChIInChI=1S/C37H50N8O5S/c1-25(2)19-32(35(46)41-31(17-18-51(3,49)50)20-27-9-13-29(23-38)14-10-27)42-36(47)33(21-28-11-15-30(24-39)16-12-28)43-37(48)34(44-45-40)22-26-7-5-4-6-8-26/h4-16,25,31-34H,17-24,38-39H2,1-3H3,(H,41,46)(H,42,47)(H,43,48)/t31-,32+,33-,34+/m1/s1
InChIKeyQRQMUCDZCOVIHS-ITHRCTNCSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01NCc1ccc(CC(CCS(C)(=O)=O)NC(=O)C(CC(C)C)NC(=O)C(Cc2ccc(CN)cc2)NC(=O)C(Cc2ccccc2)\N=[N+]=[N-])cc1
OpenEye OEToolkits 2.0.7CC(C)C[C@@H](C(=O)N[C@H](CCS(=O)(=O)C)Cc1ccc(cc1)CN)NC(=O)[C@@H](Cc2ccc(cc2)CN)NC(=O)[C@H](Cc3ccccc3)N=[N+]=[N-]
CACTVS 3.385CC(C)C[CH](NC(=O)[CH](Cc1ccc(CN)cc1)NC(=O)[CH](Cc2ccccc2)N=[N+]=[N-])C(=O)N[CH](CC[S](C)(=O)=O)Cc3ccc(CN)cc3
OpenEye OEToolkits 2.0.7CC(C)CC(C(=O)NC(CCS(=O)(=O)C)Cc1ccc(cc1)CN)NC(=O)C(Cc2ccc(cc2)CN)NC(=O)C(Cc3ccccc3)N=[N+]=[N-]
CACTVS 3.385CC(C)C[C@H](NC(=O)[C@@H](Cc1ccc(CN)cc1)NC(=O)[C@H](Cc2ccccc2)N=[N+]=[N-])C(=O)N[C@H](CC[S](C)(=O)=O)Cc3ccc(CN)cc3
FormulaC37 H50 N8 O5 S
NameN3Phe-Phe(4-NH2CH2)-Leu-Phe(4-NH2CH2)-methyl vinyl sulfone, bound form
ChEMBL
DrugBank
ZINC
PDB chain4inu Chain V Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4inu Incorporation of Non-natural Amino Acids Improves Cell Permeability and Potency of Specific Inhibitors of Proteasome Trypsin-like Sites.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		F123 D124 L125 I126 D130
Binding residue
(residue number reindexed from 1)		F123 D124 L125 I126 D130
Annotation score1
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
View graph for
Cellular Component
External links
PDB RCSB:4inu, PDBe:4inu, PDBj:4inu
PDBsum4inu
PubMed23320547
UniProtP25451|PSB3_YEAST Proteasome subunit beta type-3 (Gene Name=PUP3)

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