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Structure of PDB 3mt6 Chain H Binding Site BS02

Receptor Information
>3mt6 Chain H (length=186) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ALVPMVIEERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENP
EKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTA
GAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMAL
HTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTH
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3mt6 Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.
Resolution1.901 Å
Binding residue
(original residue number in PDB)
L48 A52 T79 F82
Binding residue
(residue number reindexed from 1)
L43 A47 T74 F77
Enzymatic activity
Catalytic site (original residue number in PDB) G68 S97 M98 H122 D171
Catalytic site (residue number reindexed from 1) G63 S92 M93 H117 D166
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:0005515 protein binding
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
GO:0009266 response to temperature stimulus
GO:0009314 response to radiation
GO:0009408 response to heat
GO:0010498 proteasomal protein catabolic process
GO:0043068 positive regulation of programmed cell death
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009368 endopeptidase Clp complex
GO:0009376 HslUV protease complex
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3mt6, PDBe:3mt6, PDBj:3mt6
PDBsum3mt6
PubMed20851345
UniProtP0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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