Structure of PDB 3otp Chain F Binding Site BS01
Receptor Information
>3otp Chain F (length=378) Species:
562
(Escherichia coli) [
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QMPSLAPMLEKVMPSVVSINVEQKFMALGSGVIIDADKGYVVTNNHVVDN
ATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALR
VGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGN
AGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQ
VKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDV
ITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSFN
GIEGAEMSNKGKDQGVVVNNVKTGTPAAQILKKGDVIIGANQQAVKNIAE
LRKVLDSKPSVLALNIQRGDSTIYLLMQ
Ligand information
>3otp Chain L (length=10) Species:
9031
(Gallus gallus) [
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WVSAAGILQI
Receptor-Ligand Complex Structure
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PDB
3otp
Covalent Linkage of Distinct Substrate Degrons Controls Assembly and Disassembly of DegP Proteolytic Cages.
Resolution
3.76 Å
Binding residue
(original residue number in PDB)
H105 L190 R207 G208 A210 T226 I228 L229 A230 E264 L265 G266 I267 M268 G269 S291 F321 L324 R325
Binding residue
(residue number reindexed from 1)
H46 L131 R148 G149 A151 T167 I169 L170 A171 E205 L206 G207 I208 M209 G210 S232 F262 L265 R266
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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Cellular Component
External links
PDB
RCSB:3otp
,
PDBe:3otp
,
PDBj:3otp
PDBsum
3otp
PubMed
21458668
UniProt
P0C0V0
|DEGP_ECOLI Periplasmic serine endoprotease DegP (Gene Name=degP)
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