Structure of PDB 6hwn Chain C

Receptor sequence
>6hwnC (length=188) Species: 274 (Thermus thermophilus) [Search protein sequence]
VIPYVIEQERVYDIYSRLLKDRIIFLGTPIDAQVANVVVAQLLFLDAQNP
NQEIKLYINSPGGEVDAGLAIYDTMQFVRAPVSTIVIGMAASMAAVILAA
GEKGRRYALPHAKVMIHQPWGGVRGTASDIAIQAQEILKAKKLLNEILAK
HTGQPLEKVEKDTDRDYYLSAQEALEYGLIDQVVTREE
3D structure
PDB6hwn Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors.
ChainC
Resolution1.95 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 C G68 E69 V70 S97 P124 W125 G63 E64 V65 S92 P119 W120
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
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)

[Back to BioLiP]