Structure of PDB 4eu2 Chain I

Receptor sequence
>4eu2I (length=222) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAA
DTEAVTQLIGSNIELHSLYTSREPRVVSALQMLKQHLFKYQGHIGAYLIV
AGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEE
AIKLASDAIQAGIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQ
KSYKFPRGTTAVLKESIVNICD
3D structure
PDB4eu2 Homopiperazine derivatives as a novel class of proteasome inhibitors with a unique mode of proteasome binding.
ChainI
Resolution2.509 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T1 D17 R19 K33 G47 S129 D166 S169
Catalytic site (residue number reindexed from 1) T1 D17 R19 K33 G47 S129 D166 S169
Enzyme Commision number 3.4.25.1: proteasome endopeptidase complex.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 WPI I T1 A46 G47 G128 S129 T1 A46 G47 G128 S129
Gene Ontology
Molecular Function
GO:0004298 threonine-type endopeptidase activity
Biological Process
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005839 proteasome core complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:4eu2, PDBe:4eu2, PDBj:4eu2
PDBsum4eu2
PubMed23593271
UniProtP25043|PSB2_YEAST Proteasome subunit beta type-2 (Gene Name=PUP1)

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