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BioLiP

Structure of PDB 6pmd Chain N Binding Site BS01

Receptor Information
>6pmd Chain N (length=182) Species: 93061 (Staphylococcus aureus subsp. aureus NCTC 8325) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LIPTVIYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDIY
LYINSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGK
RFALPNAEVMIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQS
IEKIQKDTDRDNFLTAEEAKEYGLIDEVMVPE
Ligand information
Receptor-Ligand Complex Structure
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PDB6pmd Ureadepsipeptides as ClpP Activators.
Resolution2.21 Å
Binding residue
(original residue number in PDB)
L49 F50 T80 H83
Binding residue
(residue number reindexed from 1)
L38 F39 T69 H72
Enzymatic activity
Catalytic site (original residue number in PDB) G69 S98 M99 H123 D172
Catalytic site (residue number reindexed from 1) G58 S87 M88 H112 D161
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: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:6pmd, PDBe:6pmd, PDBj:6pmd
PDBsum6pmd
PubMed31588734
UniProtQ2G036|CLPP_STAA8 ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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