Structure of PDB 3ou0 Chain A Binding Site BS02

Receptor Information

>3ou0 Chain A (length=392) Species: 562 (Escherichia coli)

QMPSLAPMLEKVMPSVVSINVEGSTQKFMALGSGVIIDADKGYVVTNNHV
VDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSD
ALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAIN
RGNAGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVE
YGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKA
GDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQ
SSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDV
IIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ

Ligand information

>3ou0 Chain C (length=7)

AAAAAAA

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3ou0 Covalent Linkage of Distinct Substrate Degrons Controls Assembly and Disassembly of DegP Proteolytic Cages.
• Resolution: 3.0 Å
• Binding residue (original residue number in PDB): L265 I267 M268 G269 F321
• Binding residue (residue number reindexed from 1): L209 I211 M212 G213 F265

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:3ou0, PDBe:3ou0, PDBj:3ou0
• PDBsum: 3ou0
• PubMed: 21458668
• UniProt: P0C0V0|DEGP_ECOLI Periplasmic serine endoprotease DegP (Gene Name=degP)