Structure of PDB 2gpl Chain I

Receptor sequence
>2gplI (length=204) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFL
GITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERRFG
PYFVGPVVAGINSKSGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCE
SLYEPNLEPEDLFETISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLK
MRQD
3D structure
PDB2gpl TMC-95-Based Inhibitor Design Provides Evidence for the Catalytic Versatility of the Proteasome.
ChainI
Resolution2.81 Å
3D
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
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 BIQ I S-5 D114 L115 S4 D124 L125
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:2gpl, PDBe:2gpl, PDBj:2gpl
PDBsum2gpl
PubMed16793518
UniProtP25451|PSB3_YEAST Proteasome subunit beta type-3 (Gene Name=PUP3)

[Back to BioLiP]