Structure of PDB 5w18 Chain E

Receptor sequence
>5w18E (length=178) Species: 93061 (Staphylococcus aureus subsp. aureus NCTC 8325) [Search protein sequence]
PTVYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDIYLYI
NSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFA
LPNAEVMIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEK
IQKDTDRDNFLTAEEAKEYGLIDEVMVP
3D structure
PDB5w18 Ureadepsipeptides as ClpP Activators.
ChainE
Resolution2.44 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) G55 S84 M85 H109 D158
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 E L49 A53 T80 L35 A39 T66
BS02 peptide E D27 I29 Y61 Y63 Q89 I91 I93 L115 M190 D13 I15 Y47 Y49 Q75 I77 I79 L101 M176
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:5w18, PDBe:5w18, PDBj:5w18
PDBsum5w18
PubMed31588734
UniProtQ2G036|CLPP_STAA8 ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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