Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0006465 | biological_process | signal peptide processing |
A | 0006508 | biological_process | proteolysis |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0016020 | cellular_component | membrane |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0006465 | biological_process | signal peptide processing |
B | 0006508 | biological_process | proteolysis |
B | 0008236 | molecular_function | serine-type peptidase activity |
B | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE JZA A 324 |
Chain | Residue |
A | SER88 |
A | SER90 |
A | ASN277 |
A | SER278 |
A | ALA279 |
A | GLU307 |
C | TYR6 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE TRT A 325 |
Chain | Residue |
A | GOL326 |
A | GLU104 |
A | THR297 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL A 326 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 327 |
Chain | Residue |
A | ARG236 |
A | GOL328 |
A | GOL329 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 328 |
Chain | Residue |
A | GLY321 |
A | ILE322 |
A | HIS323 |
A | GOL327 |
A | CCN330 |
B | ASN186 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 329 |
Chain | Residue |
A | SER317 |
A | ARG318 |
A | GOL327 |
A | HOH2127 |
A | HOH2128 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CCN A 330 |
Chain | Residue |
A | THR94 |
A | ILE322 |
A | HIS323 |
A | GOL328 |
A | CCN331 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CCN A 331 |
Chain | Residue |
A | THR94 |
A | HIS235 |
A | ARG236 |
A | HIS323 |
A | CCN330 |
A | HOH2079 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE JZA B 324 |
Chain | Residue |
B | SER88 |
B | SER90 |
B | LYS145 |
B | ASN277 |
B | SER278 |
B | ALA279 |
B | GLU307 |
B | TRT325 |
D | TYR6 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TRT B 325 |
Chain | Residue |
A | PHE196 |
B | PHE196 |
B | ASP276 |
B | ASN277 |
B | SER278 |
B | ALA279 |
B | TYR283 |
B | JZA324 |
site_id | BC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR CHAIN C OF ARYLOMYCIN A2 |
Chain | Residue |
A | GLU82 |
A | PRO83 |
A | PHE84 |
A | GLN85 |
A | PRO87 |
A | SER88 |
A | SER90 |
A | ASP142 |
A | TYR143 |
A | ILE144 |
A | LYS145 |
A | JZA324 |
A | HOH2002 |
A | HOH2024 |
A | HOH2025 |
C | HOH2002 |
site_id | BC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR CHAIN D OF ARYLOMYCIN A2 |
Chain | Residue |
B | GLU82 |
B | PRO83 |
B | PHE84 |
B | GLN85 |
B | PRO87 |
B | ASP142 |
B | TYR143 |
B | ILE144 |
B | LYS145 |
B | JZA324 |
B | HOH2020 |
B | HOH2022 |
D | HOH2001 |
D | HOH2003 |
D | HOH2004 |
Functional Information from PROSITE/UniProt
site_id | PS00501 |
Number of Residues | 8 |
Details | SPASE_I_1 Signal peptidases I serine active site. SGSMMPTL |
Chain | Residue | Details |
A | SER88-LEU95 | |
site_id | PS00760 |
Number of Residues | 13 |
Details | SPASE_I_2 Signal peptidases I lysine active site. KRAVGlPGDkVtY |
Chain | Residue | Details |
A | LYS145-TYR157 | |
site_id | PS00761 |
Number of Residues | 14 |
Details | SPASE_I_3 Signal peptidases I signature 3. YFMMGDNRdnSadS |
Chain | Residue | Details |
A | TYR268-SER281 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 492 |
Details | TOPO_DOM: Periplasmic => ECO:0000305 |
Chain | Residue | Details |
A | ARG77-HIS323 | |
B | ARG77-HIS323 | |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | SER90 | |
A | LYS145 | |
B | SER90 | |
B | LYS145 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 635 |
Chain | Residue | Details |
A | SER88 | electrostatic stabiliser |
A | SER90 | nucleofuge, nucleophile, proton acceptor, proton donor |
A | LYS145 | proton acceptor, proton donor |
A | SER278 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 635 |
Chain | Residue | Details |
B | SER88 | electrostatic stabiliser |
B | SER90 | nucleofuge, nucleophile, proton acceptor, proton donor |
B | LYS145 | proton acceptor, proton donor |
B | SER278 | electrostatic stabiliser |