Structure of PDB 3mt6 Chain L Binding Site BS02

Receptor Information

>3mt6 Chain L (length=187) Species: 83333 (Escherichia coli K-12)

LVPMVIEQGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAEN
PEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLT
AGAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMA
LHTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTH

Ligand information

>3mt6 Chain l (length=7) Species: 67305 (Streptomyces hawaiiensis)

tFSPAAK

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3mt6 Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.
• Resolution: 1.901 Å
• Binding residue (original residue number in PDB): R22 L23 E26 Y60 Y62 I90 L189
• Binding residue (residue number reindexed from 1): R18 L19 E22 Y56 Y58 I86 L185

Enzymatic activity

• Catalytic site (original residue number in PDB): G68 S97 M98 H122 D171
• Catalytic site (residue number reindexed from 1): G64 S93 M94 H118 D167
• 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:3mt6, PDBe:3mt6, PDBj:3mt6
• PDBsum: 3mt6
• PubMed: 20851345
• UniProt: P0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)