Structure of PDB 6ppe Chain J Binding Site BS01

Receptor Information

>6ppe Chain J (length=192) Species: 562 (Escherichia coli)

LVPMVIEQTSRGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLE
AENPEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAF
LLTAGAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNE
LMALHTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN

Ligand information

>6ppe Chain Y (length=9) Species: 562 (Escherichia coli)

GIGFGATVK

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6ppe Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate.
• Resolution: 3.19 Å
• Binding residue (original residue number in PDB): R22 E26 Y62 R192
• Binding residue (residue number reindexed from 1): R21 E25 Y61 R191

Enzymatic activity

• Enzyme Commision number: 3.4.21.92: endopeptidase Clp.

Gene Ontology

Molecular Function

• GO:0004176 ATP-dependent peptidase activity
• GO:0004252 serine-type endopeptidase activity
• GO:0005515 protein binding
• GO:0008236 serine-type peptidase activity
• GO:0042802 identical protein binding
• GO:0051117 ATPase binding

Biological Process

• GO:0006508 proteolysis
• GO:0006515 protein quality control for misfolded or incompletely synthesized proteins
• GO:0009266 response to temperature stimulus
• GO:0009314 response to radiation
• GO:0009408 response to heat
• GO:0010498 proteasomal protein catabolic process
• GO:0043068 positive regulation of programmed cell death

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0009368 endopeptidase Clp complex
• GO:0009376 HslUV protease complex
• GO:0016020 membrane

External links

• PDB: RCSB:6ppe, PDBe:6ppe, PDBj:6ppe
• PDBsum: 6ppe
• PubMed: 32108573
• UniProt: P0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)