Structure of PDB 6jjk Chain F Binding Site BS01
Receptor Information
>6jjk Chain F (length=379) Species:
83333
(Escherichia coli K-12) [
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QMPSLAPMLEKVMPSVVSINVEQKFMALGSGVIIDADKGYVVTNNHVVDN
ATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALR
VGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGN
AGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQ
VKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDV
ITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSFN
GIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIA
ELRKVLDSKPSVLALNIQRGDSTIYLLMQ
Ligand information
>6jjk Chain L (length=3) Species:
562
(Escherichia coli) [
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YKI
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)
H105 N206 R207 A210
Binding residue
(residue number reindexed from 1)
H46 N147 R148 A151
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
View graph for
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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