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3GDU

Crystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YRF peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0071218biological_processcellular response to misfolded protein
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
B0071218biological_processcellular response to misfolded protein
C0004252molecular_functionserine-type endopeptidase activity
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008236molecular_functionserine-type peptidase activity
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0042802molecular_functionidentical protein binding
C0071218biological_processcellular response to misfolded protein
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues981
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:11442831
ChainResidueDetails
ASER28-ASN355
BSER28-ASN355
CSER28-ASN355

site_idSWS_FT_FI2
Number of Residues9
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286
ChainResidueDetails
AHIS96
AASP126
AMIS201
BHIS96
BASP126
BMIS201
CHIS96
CASP126
CMIS201

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING:
ChainResidueDetails
ATHR184
AILE259
ATYR351
BTHR184
BILE259
BTYR351
CTHR184
CILE259
CTYR351

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ds2
ChainResidueDetails
AGLY199
AASP126
AHIS96

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ds2
ChainResidueDetails
BGLY199
BASP126
BHIS96

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ds2
ChainResidueDetails
CGLY199
CASP126
CHIS96

238268

PDB entries from 2025-07-02

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