Structure of PDB 5dl1 Chain A

Receptor sequence
>5dl1A (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.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A S98 I122 H123 Q124 P125 L126 L150 T169 S93 I117 H118 Q119 P120 L121 L145 T164 PDBbind-CN: -logKd/Ki=5.00,IC50<10uM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
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)

[Back to BioLiP]