Structure of PDB 4inu Chain I Binding Site BS01

Receptor Information
>4inu Chain I (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 H 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 C128 D130
Binding residue
(residue number reindexed from 1)		F123 D124 L125 I126 C128 D130
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=9.26,IC50=0.55nM
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

View graph for
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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