Structure of PDB 3ktk Chain N Binding Site BS02
Receptor Information
>3ktk Chain N (length=174) Species:
1423
(Bacillus subtilis) [
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DIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLAAEDPEKEISLYINSPG
GSITAGMAIYDTMQFIKPKVSTICIGMAASMGAFLLAAGEKGKRYALPNS
EVMIHQPLGGAQGQATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERD
TDRDNFKSAEEALEYGLIDKILTH
Ligand information
>3ktk Chain 1 (length=7) [
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tFSPKAP
Receptor-Ligand Complex Structure
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PDB
3ktk
Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism
Resolution
2.6 Å
Binding residue
(original residue number in PDB)
R22 D26 I28 S60 Y62 I90 I92 Y112 L114
Binding residue
(residue number reindexed from 1)
R5 D9 I11 S43 Y45 I73 I75 Y95 L97
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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Cellular Component
External links
PDB
RCSB:3ktk
,
PDBe:3ktk
,
PDBj:3ktk
PDBsum
3ktk
PubMed
20305655
UniProt
P80244
|CLPP_BACSU ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)
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