Structure of PDB 1g65 Chain N Binding Site BS01
Receptor Information
>1g65 Chain N (length=196) Species:
559292
(Saccharomyces cerevisiae S288C) [
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TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAA
DTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVA
GYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEE
TVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
1g65 Chain N Residue 201 [
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Receptor-Ligand Complex Structure
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PDB
1g65
Crystal Structure of Epoxomicin:20S Proteasome reveals a molecular basis for selectivity of alpha,beta-Epoxyketone Proteasome Inhibitors
Resolution
2.25 Å
Binding residue
(original residue number in PDB)
I163 D166 S169
Binding residue
(residue number reindexed from 1)
I163 D166 S169
Annotation score
4
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.
Gene Ontology
Molecular Function
GO:0004175
endopeptidase activity
GO:0004298
threonine-type endopeptidase activity
GO:0005515
protein binding
Biological Process
GO:0006508
proteolysis
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
GO:0034515
proteasome storage granule
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Molecular Function
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Cellular Component
External links
PDB
RCSB:1g65
,
PDBe:1g65
,
PDBj:1g65
PDBsum
1g65
PubMed
UniProt
P38624
|PSB1_YEAST Proteasome subunit beta type-1 (Gene Name=PRE3)
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