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 | 4 |
| Details | Active site: {} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1t7d |
| Chain | Residue | Details |
| A | SER90 | |
| A | LYS145 | |
| A | SER88 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1t7d |
| Chain | Residue | Details |
| B | SER90 | |
| B | LYS145 | |
| B | SER88 | |
| 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 |
