Structure of PDB 6l3x Chain C

Receptor sequence
>6l3xC (length=177) Species: 273036 (Staphylococcus aureus RF122) [Search protein sequence]
DIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDIYLYINSPG
GSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFALPNA
EVMIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKD
TDRDNFLTAEEAKEYGLIDEVMVPETK
3D structure
PDB6l3x Discovery of Novel Peptidomimetic Boronate ClpP Inhibitors with Noncanonical Enzyme Mechanism as Potent Virulence Blockersin Vitroandin Vivo.
ChainC
Resolution2.3054 Å
3D
structure
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Enzymatic activity
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 E4U C G68 G69 S70 V71 S98 M99 H123 P125 L126 G127 G50 G51 S52 V53 S80 M81 H105 P107 L108 G109
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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Cellular Component
External links
PDB RCSB:6l3x, PDBe:6l3x, PDBj:6l3x
PDBsum6l3x
PubMed32031798
UniProtQ2YSF8|CLPP_STAAB ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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