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1T7D

Crystal structure of Escherichia coli type I signal peptidase in complex with a lipopeptide inhibitor

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 PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR CHAIN C OF ARYLOMYCIN A2
ChainResidue
AGLU82
AHOH2005
AHOH2006
APRO83
AGLN85
APRO87
ASER90
AASP142
ATYR143
AILE144
ALYS145

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR CHAIN D OF ARYLOMYCIN A2
ChainResidue
BPRO83
BPHE84
BGLN85
BPRO87
BSER88
BSER90
BASP142
BTYR143
BILE144
BLYS145
DHOH2002
DHOH2003

Functional Information from PROSITE/UniProt
site_idPS00501
Number of Residues8
DetailsSPASE_I_1 Signal peptidases I serine active site. SGSMMPTL
ChainResidueDetails
ASER88-LEU95

site_idPS00760
Number of Residues13
DetailsSPASE_I_2 Signal peptidases I lysine active site. KRAVGlPGDkVtY
ChainResidueDetails
ALYS145-TYR157

site_idPS00761
Number of Residues14
DetailsSPASE_I_3 Signal peptidases I signature 3. YFMMGDNRdnSadS
ChainResidueDetails
ATYR268-SER281

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues492
DetailsTOPO_DOM: Periplasmic => ECO:0000305
ChainResidueDetails
AARG77-HIS323
BARG77-HIS323

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE:
ChainResidueDetails
ASER90
ALYS145
BSER90
BLYS145

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 635
ChainResidueDetails
ASER88electrostatic stabiliser
ASER90nucleofuge, nucleophile, proton acceptor, proton donor
ALYS145proton acceptor, proton donor
ASER278electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 635
ChainResidueDetails
BSER88electrostatic stabiliser
BSER90nucleofuge, nucleophile, proton acceptor, proton donor
BLYS145proton acceptor, proton donor
BSER278electrostatic stabiliser

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PDB entries from 2024-04-24

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