Structure of PDB 7fep Chain N Binding Site BS01
Receptor Information
>7fep Chain N (length=189) Species:
1423
(Bacillus subtilis) [
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LIPTVIEQTNRGERAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLA
AEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTICIGMAASMGAF
LLAAGEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILLLRDKLNK
VLAERTGQPLEVIERDTDRDNFKSAEEALEYGLIDKILT
Ligand information
>7fep Chain Y (length=7) Species:
32630
(synthetic construct) [
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tFSPAAK
Receptor-Ligand Complex Structure
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PDB
7fep
Structural insights into ClpP protease side exit pore-opening by a pH drop coupled with substrate hydrolysis.
Resolution
3.1 Å
Binding residue
(original residue number in PDB)
R22 D26 Y62
Binding residue
(residue number reindexed from 1)
R21 D25 Y61
Enzymatic activity
Enzyme Commision number
3.4.21.92
: endopeptidase Clp.
Gene Ontology
Molecular Function
GO:0004176
ATP-dependent peptidase activity
GO:0004252
serine-type endopeptidase activity
GO:0008236
serine-type peptidase activity
GO:0042802
identical protein binding
GO:0051117
ATPase binding
Biological Process
GO:0006508
proteolysis
GO:0006515
protein quality control for misfolded or incompletely synthesized proteins
Cellular Component
GO:0005737
cytoplasm
GO:0009368
endopeptidase Clp complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:7fep
,
PDBe:7fep
,
PDBj:7fep
PDBsum
7fep
PubMed
35593068
UniProt
P80244
|CLPP_BACSU ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)
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