Structure of PDB 3ktj Chain E

Receptor sequence
>3ktjE (length=174) Species: 1423 (Bacillus subtilis) [Search protein sequence]
DIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLAAEDPEKEISLYINSPG
GSITAGMAIYDTMQFIKPKVSTICIGMAASMGAFLLAAGEKGKRYALPNS
EVMIHQPLGGAQGQATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERD
TDRDNFKSAEEALEYGLIDKILTH
3D structure
PDB3ktj Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism
ChainE
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) G68 S97 M98 H122 D171
Catalytic site (residue number reindexed from 1) G51 S80 M81 H105 D154
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 E L48 A52 T79 F82 L31 A35 T62 F65
BS02 peptide E D26 Y62 I90 I92 L114 D9 Y45 I73 I75 L97
Gene Ontology
Molecular Function
GO:0004176 ATP-dependent peptidase activity
GO:0004252 serine-type endopeptidase activity
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
Cellular Component
GO:0005737 cytoplasm
GO:0009368 endopeptidase Clp complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3ktj, PDBe:3ktj, PDBj:3ktj
PDBsum3ktj
PubMed20305655
UniProtP80244|CLPP_BACSU ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

[Back to BioLiP]