Structure of PDB 3kti Chain E Binding Site BS02

Receptor Information
>3kti Chain E (length=174) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLAAEDPEKEISLYINSPG
GSITAGMAIYDTMQFIKPKVSTICIGMAASMGAFLLAAGEKGKRYALPNS
EVMIHQPLGGAQGQATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERD
TDRDNFKSAEEALEYGLIDKILTH
Ligand information
Receptor-Ligand Complex Structure
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PDB3kti Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism
Resolution2.0 Å
Binding residue
(original residue number in PDB)		D26 I28 S60 Y62 I90 Y112 L114 L189
Binding residue
(residue number reindexed from 1)		D9 I11 S43 Y45 I73 Y95 L97 L172
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3kti, PDBe:3kti, PDBj:3kti
PDBsum3kti
PubMed20305655
UniProtP80244|CLPP_BACSU ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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