Structure of PDB 1ryp Chain Z Binding Site BS01

Receptor Information
>1ryp Chain Z (length=212) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKRVIEINPFLLGTMAGGAA
DCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTM
ICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSV
EDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKV
KEEEGSFNNVIG
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1ryp Chain Z Residue 213 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ryp Structure of 20S proteasome from yeast at 2.4 A resolution.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		A165 D168 S171
Binding residue
(residue number reindexed from 1)		A165 D168 S171
Annotation score4
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.
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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Biological Process
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Cellular Component
External links
PDB RCSB:1ryp, PDBe:1ryp, PDBj:1ryp
PDBsum1ryp
PubMed9087403
UniProtP30656|PSB5_YEAST Proteasome subunit beta type-5 (Gene Name=PRE2)

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