Structure of PDB 3ou0 Chain A

Receptor sequence
>3ou0A (length=392) Species: 562 (Escherichia coli) [Search protein sequence]
QMPSLAPMLEKVMPSVVSINVEGSTQKFMALGSGVIIDADKGYVVTNNHV
VDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSD
ALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAIN
RGNAGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVE
YGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKA
GDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQ
SSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDV
IIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ
3D structure
PDB3ou0 Covalent Linkage of Distinct Substrate Degrons Controls Assembly and Disassembly of DegP Proteolytic Cages.
ChainA
Resolution3.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.21.107: peptidase Do.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide A H105 A210 I228 L229 A230 H49 A154 I172 L173 A174
BS02 peptide A L265 I267 M268 G269 F321 L209 I211 M212 G213 F265
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:3ou0, PDBe:3ou0, PDBj:3ou0
PDBsum3ou0
PubMed21458668
UniProtP0C0V0|DEGP_ECOLI Periplasmic serine endoprotease DegP (Gene Name=degP)

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