Structure of PDB 5dkp Chain E Binding Site BS02
Receptor Information
>5dkp Chain E (length=192) Species:
122586
(Neisseria meningitidis MC58) [
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YLVPTVIEQSGRGERAFDIYSRLLKERIVFLVGPVTDESANLVVAQLLFL
ESENPDKDIFFYINSPGGSVTAGMSIYDTMNFIKPDVSTLCLGQAASMGA
FLLSAGEKGKRFALPNSRIMIHQPLISGGLGGQASDIEIHARELLKIKEK
LNRLMAKHCDRDLADLERDTDRDNFMSAEEAKEYGLIDQILE
Ligand information
>5dkp Chain T (length=7) Species:
32630
(synthetic construct) [
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tFSPAAK
Receptor-Ligand Complex Structure
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PDB
5dkp
Development and Characterization of Potent Cyclic Acyldepsipeptide Analogues with Increased Antimicrobial Activity.
Resolution
2.381 Å
Binding residue
(original residue number in PDB)
S57 F87
Binding residue
(residue number reindexed from 1)
S52 F82
Enzymatic activity
Catalytic site (original residue number in PDB)
G73 S102 M103 H127 D178
Catalytic site (residue number reindexed from 1)
G68 S97 M98 H122 D173
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: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
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Biological Process
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Cellular Component
External links
PDB
RCSB:5dkp
,
PDBe:5dkp
,
PDBj:5dkp
PDBsum
5dkp
PubMed
26818454
UniProt
Q9JZ38
|CLPP_NEIMB ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)
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