Structure of PDB 3ktk Chain J Binding Site BS02

Receptor Information

>3ktk Chain J (length=174) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

DIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLAAEDPEKEISLYINSPG
GSITAGMAIYDTMQFIKPKVSTICIGMAASMGAFLLAAGEKGKRYALPNS
EVMIHQPLGGAQGQATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERD
TDRDNFKSAEEALEYGLIDKILTH

Ligand information

>3ktk Chain Z (length=7) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

tFSPKAP

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	3ktk Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism
Resolution	2.6 Å
Binding residue (original residue number in PDB)	L48 T79 F82
Binding residue (residue number reindexed from 1)	L31 T62 F65

Enzymatic activity

Enzyme Commision number

3.4.21.92: endopeptidase Clp.

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:3ktk, PDBe:3ktk, PDBj:3ktk
PDBsum	3ktk
PubMed	20305655
UniProt	P80244\|CLPP_BACSU ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

[Back to BioLiP]