Structure of PDB 6jjo Chain F Binding Site BS01

Receptor Information

>6jjo Chain F (length=379) Species: 83333 (Escherichia coli K-12)

QMPSLAPMLEKVMPSVVSINVEQKFMALGSGVIIDADKGYVVTNNHVVDN
ATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALR
VGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGN
AGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQ
VKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDV
ITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSFN
GIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIA
ELRKVLDSKPSVLALNIQRGDSTIYLLMQ

Ligand information

>6jjo Chain L (length=5) Species: 562 (Escherichia coli)

CYRKL

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6jjo Over-activation of a nonessential bacterial protease DegP as an antibiotic strategy
• Resolution: 4.157 Å
• Binding residue (original residue number in PDB): H105 L190 A227
• Binding residue (residue number reindexed from 1): H46 L131 A168

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

External links

• PDB: RCSB:6jjo, PDBe:6jjo, PDBj:6jjo
• PDBsum: 6jjo
• PubMed: 33005001
• UniProt: P0C0V0|DEGP_ECOLI Periplasmic serine endoprotease DegP (Gene Name=degP)