Structure of PDB 6jjk Chain B Binding Site BS02
Receptor Information
>6jjk Chain B (length=392) Species:
83333
(Escherichia coli K-12) [
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QMPSLAPMLEKVMPSVVSINVEGSTQKFMALGSGVIIDADKGYVVTNNHV
VDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSD
ALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAIN
RGNAGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVE
YGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKA
GDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQ
SSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDV
IIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ
Ligand information
>6jjk Chain N (length=5) Species:
562
(Escherichia coli) [
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CYYKI
Receptor-Ligand Complex Structure
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PDB
6jjk
Over-activation of a nonessential bacterial protease DegP as an antibiotic strategy
Resolution
3.6 Å
Binding residue
(original residue number in PDB)
I267 M268 G269 T270 S291 F321 V328
Binding residue
(residue number reindexed from 1)
I211 M212 G213 T214 S235 F265 V272
Enzymatic activity
Enzyme Commision number
3.4.21.107
: peptidase Do.
Gene Ontology
Molecular Function
GO:0004175
endopeptidase activity
GO:0004252
serine-type endopeptidase activity
GO:0005515
protein binding
GO:0008233
peptidase activity
GO:0008236
serine-type peptidase activity
GO:0042802
identical protein binding
Biological Process
GO:0006457
protein folding
GO:0006508
proteolysis
GO:0006515
protein quality control for misfolded or incompletely synthesized proteins
GO:0006979
response to oxidative stress
GO:0009266
response to temperature stimulus
GO:0009408
response to heat
GO:0061077
chaperone-mediated protein folding
Cellular Component
GO:0005886
plasma membrane
GO:0030288
outer membrane-bounded periplasmic space
GO:0042597
periplasmic space
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6jjk
,
PDBe:6jjk
,
PDBj:6jjk
PDBsum
6jjk
PubMed
33005001
UniProt
P0C0V0
|DEGP_ECOLI Periplasmic serine endoprotease DegP (Gene Name=degP)
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