Structure of PDB 3mt6 Chain Y

Receptor sequence
>3mt6Y (length=186) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LVPMVIEQTRSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENP
EKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTA
GAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMAL
HTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTH
3D structure
PDB3mt6 Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.
ChainY
Resolution1.901 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) G63 S92 M93 H117 D166
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 Y L48 A52 T79 F82 L43 A47 T74 F77
BS02 peptide Y R22 E26 Y60 Y62 I90 L189 R17 E21 Y55 Y57 I85 L184
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:3mt6, PDBe:3mt6, PDBj:3mt6
PDBsum3mt6
PubMed20851345
UniProtP0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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