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BioLiP

Structure of PDB 3mh7 Chain A Binding Site BS02

Receptor Information
>3mh7 Chain A (length=392) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QMPSLAPMLEKVMPSVVSINVEGSTQKFMALGSGVIIDADKGYVVTNNHV
VDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSD
ALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAIN
RGNAGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVE
YGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKA
GDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQ
SSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDV
IIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3mh7 HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
Resolution2.961 Å
Binding residue
(original residue number in PDB)		L265 G266 I267 M268 G269 F321
Binding residue
(residue number reindexed from 1)		L209 G210 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3mh7, PDBe:3mh7, PDBj:3mh7
PDBsum3mh7
PubMed20581825
UniProtP0C0V0|DEGP_ECOLI Periplasmic serine endoprotease DegP (Gene Name=degP)

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