Structure of PDB 4qvl Chain H

Receptor sequence
>4qvlH (length=226) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAA
DTEAVTQLIGSNIELHSLYTSREPRVVSALQMLKQHLFKYQGHIGAYLIV
AGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEE
AIKLASDAIQAGIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQ
KSYKFPRGTTAVLKESIVNICDIQEE
3D structure
PDB4qvl Bortezomib-Resistant Mutant Proteasomes: Structural and Biochemical Evaluation with Carfilzomib and ONX 0914.
ChainH
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 BO2 H T1 S20 T21 G47 A49 T1 S20 T21 G47 A49 PDBbind-CN: -logKd/Ki=6.53,IC50=0.298uM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4qvl, PDBe:4qvl, PDBj:4qvl
PDBsum4qvl
PubMed25599643
UniProtP25043|PSB2_YEAST Proteasome subunit beta type-2 (Gene Name=PUP1)

[Back to BioLiP]