Structure of PDB 5fgf Chain Y Binding Site BS01

Receptor Information
>5fgf Chain Y (length=214) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AGATTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGG
AADCQFWETWLGSQCRLHELREKERISVAAASRILSNLVYQYKGAGLSMG
TMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDL
SVEDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFW
KVKEEEGSFNNVIG
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 chain5fgf Chain I Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5fgf A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome.
Resolution2.6 Å
Binding residue
(original residue number in PDB)
A165 D168 A169 S171
Binding residue
(residue number reindexed from 1)
A167 D170 A171 S173
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) A1 D17 R19 K33 G47 S131 D168 S171
Catalytic site (residue number reindexed from 1) A3 D19 R21 K35 G49 S133 D170 S173
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:5fgf, PDBe:5fgf, PDBj:5fgf
PDBsum5fgf
PubMed26964885
UniProtP30656|PSB5_YEAST Proteasome subunit beta type-5 (Gene Name=PRE2)

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