Structure of PDB 6hwn Chain E Binding Site BS01
Receptor Information
>6hwn Chain E (length=186) Species:
274
(Thermus thermophilus) [
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IPYVIERVYDIYSRLLKDRIIFLGTPIDAQVANVVVAQLLFLDAQNPNQE
IKLYINSPGGEVDAGLAIYDTMQFVRAPVSTIVIGMAASMAAVILAAGEK
GRRYALPHAKVMIHQPWGGVRGTASDIAIQAQEILKAKKLLNEILAKHTG
QPLEKVEKDTDRDYYLSAQEALEYGLIDQVVTREEA
Ligand information
>6hwn Chain L (length=3) Species:
274
(Thermus thermophilus) [
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AAA
Receptor-Ligand Complex Structure
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PDB
6hwn
Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors.
Resolution
1.95 Å
Binding residue
(original residue number in PDB)
G68 V70 S97 M98 P124 W125
Binding residue
(residue number reindexed from 1)
G60 V62 S89 M90 P116 W117
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: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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Biological Process
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Cellular Component
External links
PDB
RCSB:6hwn
,
PDBe:6hwn
,
PDBj:6hwn
PDBsum
6hwn
PubMed
31517045
UniProt
Q5SKM8
|CLPP_THET8 ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)
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