Structure of PDB 4inr Chain I Binding Site BS01

Receptor Information
>4inr 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 ID1G1
InChIInChI=1S/C33H49N7O5S/c1-22(2)17-28(31(41)36-27(15-16-46(5,44)45)19-25-11-13-26(21-34)14-12-25)37-32(42)29(18-23(3)4)38-33(43)30(39-40-35)20-24-9-7-6-8-10-24/h6-14,22-23,27-30H,15-21,34H2,1-5H3,(H,36,41)(H,37,42)(H,38,43)/t27-,28+,29+,30+/m1/s1
InChIKeyJORBDDYVSOOLMV-RYTSNQFKSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7CC(C)CC(C(=O)NC(CC(C)C)C(=O)NC(CCS(=O)(=O)C)Cc1ccc(cc1)CN)NC(=O)C(Cc2ccccc2)N=[N+]=[N-]
CACTVS 3.385CC(C)C[CH](NC(=O)[CH](CC(C)C)NC(=O)[CH](Cc1ccccc1)N=[N+]=[N-])C(=O)N[CH](CC[S](C)(=O)=O)Cc2ccc(CN)cc2
CACTVS 3.385CC(C)C[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)N=[N+]=[N-])C(=O)N[C@H](CC[S](C)(=O)=O)Cc2ccc(CN)cc2
OpenEye OEToolkits 2.0.7CC(C)C[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](CCS(=O)(=O)C)Cc1ccc(cc1)CN)NC(=O)[C@H](Cc2ccccc2)N=[N+]=[N-]
ACDLabs 12.01NCc1ccc(CC(CCS(C)(=O)=O)NC(=O)C(CC(C)C)NC(=O)C(CC(C)C)NC(=O)C(Cc2ccccc2)/N=[N+]=[N-])cc1
FormulaC33 H49 N7 O5 S
NameN3Phe-Leu-Leu-Phe(4-NH2CH2)-methyl vinyl sulfone, bound form
ChEMBL
DrugBank
ZINC
PDB chain4inr 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

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4inr Incorporation of Non-natural Amino Acids Improves Cell Permeability and Potency of Specific Inhibitors of Proteasome Trypsin-like Sites.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		D124 I126
Binding residue
(residue number reindexed from 1)		D124 I126
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=5.59,IC50=2.6uM
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4inr, PDBe:4inr, PDBj:4inr
PDBsum4inr
PubMed23320547
UniProtP25451|PSB3_YEAST Proteasome subunit beta type-3 (Gene Name=PUP3)

[Back to BioLiP]