Structure of PDB 6wr2 Chain I

Receptor sequence

>6wr2I (length=192) Species: 83333 (Escherichia coli K-12)

LVPMVIEQTSRGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLE
AENPEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAF
LLTAGAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNE
LMALHTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN

3D structure

• PDB: 6wr2 Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates.
• Chain: I
• Resolution: 2.88 Å

Enzymatic activity

• 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	I	R22 E26 Y62 M92 R192	R21 E25 Y61 M91 R191
BS02	peptide	I	L48 A52 F82 K84	L47 A51 F81 K83

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:6wr2, PDBe:6wr2, PDBj:6wr2
• PDBsum: 6wr2
• PubMed: 33089779
• UniProt: P0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)