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BioLiP

Structure of PDB 6jjo Chain A Binding Site BS02

Receptor Information
>6jjo Chain A (length=381) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AQQMPSLAPMLEKVMPSVVSINVEQKFMALGSGVIIDADKGYVVTNNHVV
DNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDA
LRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINR
GNAGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEY
GQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAG
DVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQS
FNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKN
IAELRKVLDSKPSVLALNIQRGDSTIYLLMQ
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6jjo Over-activation of a nonessential bacterial protease DegP as an antibiotic strategy
Resolution4.157 Å
Binding residue
(original residue number in PDB)		I267 M268 G269 T270
Binding residue
(residue number reindexed from 1)		I210 M211 G212 T213
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:6jjo, PDBe:6jjo, PDBj:6jjo
PDBsum6jjo
PubMed33005001
UniProtP0C0V0|DEGP_ECOLI Periplasmic serine endoprotease DegP (Gene Name=degP)

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