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3S04

Crystal structure of Escherichia coli type I signal peptidase in complex with an Arylomycin Lipoglycopeptide Antibiotic

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006465biological_processsignal peptide processing
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0016020cellular_componentmembrane
B0004252molecular_functionserine-type endopeptidase activity
B0006465biological_processsignal peptide processing
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00501
Number of Residues8
DetailsSPASE_I_1 Signal peptidases I serine active site. SGSMMPTL
ChainResidueDetails
ASER89-LEU96

site_idPS00760
Number of Residues13
DetailsSPASE_I_2 Signal peptidases I lysine active site. KRAVGlPGDkVtY
ChainResidueDetails
ALYS146-TYR158

site_idPS00761
Number of Residues14
DetailsSPASE_I_3 Signal peptidases I signature 3. YFMMGDNRdnSadS
ChainResidueDetails
ATYR269-SER282

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 635
ChainResidueDetails
ASER89electrostatic stabiliser
ASER91nucleofuge, nucleophile, proton acceptor, proton donor
ALYS146proton acceptor, proton donor
ASER279electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 635
ChainResidueDetails
BSER89electrostatic stabiliser
BSER91nucleofuge, nucleophile, proton acceptor, proton donor
BLYS146proton acceptor, proton donor
BSER279electrostatic stabiliser

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PDB entries from 2025-12-17

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