Structure of PDB 6pka Chain A

Receptor sequence
>6pkaA (length=179) Species: 93061 (Staphylococcus aureus subsp. aureus NCTC 8325) [Search protein sequence]
IPTVYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDIYLY
INSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRF
ALPNAEVMIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIE
KIQKDTDRDNFLTAEEAKEYGLIDEVMVP
3D structure
PDB6pka Ureadepsipeptides as ClpP Activators.
ChainA
Resolution2.25 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) G56 S85 M86 H110 D159
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 peptide A D27 I29 Y61 Y63 Q89 L115 D14 I16 Y48 Y50 Q76 L102
BS02 peptide A L49 A53 T80 H83 L36 A40 T67 H70
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:6pka, PDBe:6pka, PDBj:6pka
PDBsum6pka
PubMed31588734
UniProtQ2G036|CLPP_STAA8 ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

[Back to BioLiP]