Structure of PDB 6hwn Chain E

Receptor sequence
>6hwnE (length=186) Species: 274 (Thermus thermophilus) [Search protein sequence]
IPYVIERVYDIYSRLLKDRIIFLGTPIDAQVANVVVAQLLFLDAQNPNQE
IKLYINSPGGEVDAGLAIYDTMQFVRAPVSTIVIGMAASMAAVILAAGEK
GRRYALPHAKVMIHQPWGGVRGTASDIAIQAQEILKAKKLLNEILAKHTG
QPLEKVEKDTDRDYYLSAQEALEYGLIDQVVTREEA
3D structure
PDB6hwn Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors.
ChainE
Resolution1.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.21.92: endopeptidase Clp.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide E G68 V70 S97 M98 P124 W125 G60 V62 S89 M90 P116 W117
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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Molecular Function
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Cellular Component
External links
PDB RCSB:6hwn, PDBe:6hwn, PDBj:6hwn
PDBsum6hwn
PubMed31517045
UniProtQ5SKM8|CLPP_THET8 ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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