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3MH6

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

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0051603biological_processproteolysis involved in protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DFP A 500
ChainResidue
ALEU87
AILE228
AHIS105
AASN206
AARG207
AGLY208
AASN209
ASER210
ATHR226
AALA227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues91
DetailsDomain: {"description":"PDZ 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00143","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues89
DetailsDomain: {"description":"PDZ 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00143","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"20581825","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues13
DetailsBinding site: {}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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