Structure of PDB 7fep Chain H

Receptor sequence
>7fepH (length=189) Species: 1423 (Bacillus subtilis) [Search protein sequence]
LIPTVIEQTNRGERAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLA
AEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTICIGMAASMGAF
LLAAGEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILLLRDKLNK
VLAERTGQPLEVIERDTDRDNFKSAEEALEYGLIDKILT
3D structure
PDB7fep Structural insights into ClpP protease side exit pore-opening by a pH drop coupled with substrate hydrolysis.
ChainH
Resolution3.1 Å
3D
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
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 H R22 D26 Y62 I90 Y112 R21 D25 Y61 I89 Y111
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:7fep, PDBe:7fep, PDBj:7fep
PDBsum7fep
PubMed35593068
UniProtP80244|CLPP_BACSU ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

[Back to BioLiP]