Structure of PDB 3ktj Chain F Binding Site BS01
Receptor Information
>3ktj Chain F (length=174) Species:
1423
(Bacillus subtilis) [
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DIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLAAEDPEKEISLYINSPG
GSITAGMAIYDTMQFIKPKVSTICIGMAASMGAFLLAAGEKGKRYALPNS
EVMIHQPLGGAQGQATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERD
TDRDNFKSAEEALEYGLIDKILTH
Ligand information
>3ktj Chain J (length=7) [
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tFSPKAP
Receptor-Ligand Complex Structure
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PDB
3ktj
Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism
Resolution
2.6 Å
Binding residue
(original residue number in PDB)
D26 I28 Y62 Y112
Binding residue
(residue number reindexed from 1)
D9 I11 Y45 Y95
Enzymatic activity
Catalytic site (original residue number in PDB)
G68 S97 M98 H122 D171
Catalytic site (residue number reindexed from 1)
G51 S80 M81 H105 D154
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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Cellular Component
External links
PDB
RCSB:3ktj
,
PDBe:3ktj
,
PDBj:3ktj
PDBsum
3ktj
PubMed
20305655
UniProt
P80244
|CLPP_BACSU ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)
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