Structure of PDB 3mh7 Chain A Binding Site BS01

Receptor Information

>3mh7 Chain A (length=392) Species: 83333 (Escherichia coli K-12)

QMPSLAPMLEKVMPSVVSINVEGSTQKFMALGSGVIIDADKGYVVTNNHV
VDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSD
ALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAIN
RGNAGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVE
YGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKA
GDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQ
SSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDV
IIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ

Ligand information

>3mh7 Chain B (length=5) Species: 83333 (Escherichia coli K-12)

AAAAA

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3mh7 HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
• Resolution: 2.961 Å
• Binding residue (original residue number in PDB): H105 N206 R207 G208 A210 T226 A227 I228 L229 A230
• Binding residue (residue number reindexed from 1): H49 N150 R151 G152 A154 T170 A171 I172 L173 A174

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:3mh7, PDBe:3mh7, PDBj:3mh7
• PDBsum: 3mh7
• PubMed: 20581825
• UniProt: P0C0V0|DEGP_ECOLI Periplasmic serine endoprotease DegP (Gene Name=degP)