Structure of PDB 2fzs Chain I

Receptor sequence

>2fzsI (length=183) Species: 562 (Escherichia coli)

LVPMVSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKDIY
LYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAKGK
RFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTGQS
LEQIERDTERDRFLSAPEAVEYGLVDSILTHRN

3D structure

• PDB: 2fzs Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site.
• Chain: I
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G68 S97 M98 H122 D171
• Catalytic site (residue number reindexed from 1): G58 S87 M88 H112 D161
• 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	CMQ	I	G68 V69 I70 S97 M98 H122 P124 L125 I142 M149	G58 V59 I60 S87 M88 H112 P114 L115 I132 M139

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:2fzs, PDBe:2fzs, PDBj:2fzs
• PDBsum: 2fzs
• PubMed: 16682229
• UniProt: P0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)