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3MH5

HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006457biological_processprotein folding
A0006508biological_processproteolysis
A0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
A0006979biological_processresponse to oxidative stress
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0009266biological_processresponse to temperature stimulus
A0009408biological_processresponse to heat
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0061077biological_processchaperone-mediated protein folding
B0004175molecular_functionendopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006457biological_processprotein folding
B0006508biological_processproteolysis
B0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
B0006979biological_processresponse to oxidative stress
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0009266biological_processresponse to temperature stimulus
B0009408biological_processresponse to heat
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
B0061077biological_processchaperone-mediated protein folding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DFP A 500
ChainResidue
ATHR176
AALA204
AILE205
AASN209
ASER210
AGLY211

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DFP B 500
ChainResidue
BTHR178
BALA204
BILE205
BASN209
BSER210
BGLY237
BALA166
BPRO170
BTHR176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:20581825
ChainResidueDetails
AHIS105
AASP135
ASER210
BHIS105
BASP135
BSER210

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AGLU32
BGLY208
BTHR226
BLEU265
AHIS105
AASP135
AGLY208
ATHR226
ALEU265
BGLU32
BHIS105
BASP135

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PDB entries from 2024-07-10

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