Structure of PDB 6jjk Chain A Binding Site BS01

Receptor Information
>6jjk 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
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PDB6jjk Over-activation of a nonessential bacterial protease DegP as an antibiotic strategy
Resolution3.6 Å
Binding residue
(original residue number in PDB)
L190 N206 R207 A210 T226 A227 I228 L229
Binding residue
(residue number reindexed from 1)
L133 N149 R150 A153 T169 A170 I171 L172
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
PDBsum6jjk
PubMed33005001
UniProtP0C0V0|DEGP_ECOLI Periplasmic serine endoprotease DegP (Gene Name=degP)

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