Structure of PDB 2fzs Chain D

Receptor sequence
>2fzsD (length=185) Species: 562 (Escherichia coli) [Search protein sequence]
LVPMVIESFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKD
IYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAK
GKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTG
QSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN
3D structure
PDB2fzs Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site.
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G68 S97 M98 H122 D171
Catalytic site (residue number reindexed from 1) G60 S89 M90 H114 D163
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 D G67 G68 V69 I70 S97 M98 H122 P124 L125 I142 M149 G59 G60 V61 I62 S89 M90 H114 P116 L117 I134 M141
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

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Cellular Component
External links
PDB RCSB:2fzs, PDBe:2fzs, PDBj:2fzs
PDBsum2fzs
PubMed16682229
UniProtP0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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