Structure of PDB 5dl1 Chain I

Receptor sequence
>5dl1I (length=188) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
LIPTVIETTERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQD
SEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLA
AGAKGKRFALPNAEVMIHQPLGGAQGQATEIEIAANHILKTREKLNRILS
ERTGQSIEKIQKDTDRDNFLTAEEAKEYGLIDEVMVPE
3D structure
PDB5dl1 Reversible Inhibitors Arrest ClpP in a Defined Conformational State that Can Be Revoked by ClpX Association.
ChainI
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G69 S98 M99 H123 D172
Catalytic site (residue number reindexed from 1) G64 S93 M94 H118 D167
Enzyme Commision number 3.4.21.92: endopeptidase Clp.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 5C2 I V71 S98 Q124 L126 Q132 H142 T146 R147 L150 N151 L154 T169 V66 S93 Q119 L121 Q127 H137 T141 R142 L145 N146 L149 T164
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:5dl1, PDBe:5dl1, PDBj:5dl1
PDBsum5dl1
PubMed26566002
UniProtQ2G036|CLPP_STAA8 ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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