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3IIQ

Crystallographic analysis of bacterial signal peptidase in ternary complex with Arylomycin A2 and a beta-sultam 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 Residues7
DetailsBINDING SITE FOR RESIDUE JZA A 324
ChainResidue
ASER88
ASER90
AASN277
ASER278
AALA279
AGLU307
CTYR6

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TRT A 325
ChainResidue
AGOL326
AGLU104
ATHR297

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 326
ChainResidue
ATRT325

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 327
ChainResidue
AARG236
AGOL328
AGOL329

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 328
ChainResidue
AGLY321
AILE322
AHIS323
AGOL327
ACCN330
BASN186

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 329
ChainResidue
ASER317
AARG318
AGOL327
AHOH2127
AHOH2128

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CCN A 330
ChainResidue
ATHR94
AILE322
AHIS323
AGOL328
ACCN331

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CCN A 331
ChainResidue
ATHR94
AHIS235
AARG236
AHIS323
ACCN330
AHOH2079

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE JZA B 324
ChainResidue
BSER88
BSER90
BLYS145
BASN277
BSER278
BALA279
BGLU307
BTRT325
DTYR6

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRT B 325
ChainResidue
APHE196
BPHE196
BASP276
BASN277
BSER278
BALA279
BTYR283
BJZA324

site_idBC2
Number of Residues16
DetailsBINDING SITE FOR CHAIN C OF ARYLOMYCIN A2
ChainResidue
AGLU82
APRO83
APHE84
AGLN85
APRO87
ASER88
ASER90
AASP142
ATYR143
AILE144
ALYS145
AJZA324
AHOH2002
AHOH2024
AHOH2025
CHOH2002

site_idBC3
Number of Residues15
DetailsBINDING SITE FOR CHAIN D OF ARYLOMYCIN A2
ChainResidue
BGLU82
BPRO83
BPHE84
BGLN85
BPRO87
BASP142
BTYR143
BILE144
BLYS145
BJZA324
BHOH2020
BHOH2022
DHOH2001
DHOH2003
DHOH2004

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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