Structure of PDB 5vz2 Chain E

Receptor sequence
>5vz2E (length=178) Species: 93061 (Staphylococcus aureus subsp. aureus NCTC 8325) [Search protein sequence]
PTVDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDIYLYIN
SPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFAL
PNAEVMIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEKI
QKDTDRDNFLTAEEAKEYGLIDEVMVPE
3D structure
PDB5vz2 Ureadepsipeptides as ClpP Activators.
ChainE
Resolution2.26 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) G54 S83 M84 H108 D157
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 T80 H83 T65 H68
BS02 peptide E D27 I29 Y61 Y63 M190 D12 I14 Y46 Y48 M175
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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External links
PDB RCSB:5vz2, PDBe:5vz2, PDBj:5vz2
PDBsum5vz2
PubMed31588734
UniProtQ2G036|CLPP_STAA8 ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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