Structure of PDB 1ryp Chain L

Receptor sequence
>1rypL (length=212) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKRVIEINPFLLGTMAGGAA
DCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTM
ICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSV
EDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKV
KEEEGSFNNVIG
3D structure
PDB1ryp Structure of 20S proteasome from yeast at 2.4 A resolution.
ChainL
Resolution1.9 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 R33 G47 S131 D168 S171
Catalytic site (residue number reindexed from 1) T1 D17 R19 R33 G47 S131 D168 S171
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 MG L A165 D168 S171 A165 D168 S171
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:1ryp, PDBe:1ryp, PDBj:1ryp
PDBsum1ryp
PubMed9087403
UniProtP30656|PSB5_YEAST Proteasome subunit beta type-5 (Gene Name=PRE2)

[Back to BioLiP]