Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B1568 |
| Chain | Residue |
| A | GLU152 |
| B | ASP73 |
| B | VAL75 |
| B | ASP76 |
| B | PRO205 |
| B | ASP252 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A1210 |
| Chain | Residue |
| A | ILE153 |
| A | HOH2192 |
| B | ILE77 |
| A | THR150 |
| A | SER151 |
| A | GLU152 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B1558 |
| Chain | Residue |
| B | ASP327 |
| B | ILE329 |
| B | LEU331 |
| B | EDO1560 |
| B | HOH2504 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B1559 |
| Chain | Residue |
| B | ASP293 |
| B | LEU294 |
| B | ASN295 |
| B | GLY375 |
| B | TYR376 |
| B | ASN388 |
| B | HOH2505 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B1560 |
| Chain | Residue |
| B | GLN288 |
| B | ARG291 |
| B | ILE329 |
| B | EDO1558 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1561 |
| Chain | Residue |
| A | GLN37 |
| A | ASP38 |
| B | SER508 |
| B | PHE510 |
| B | ASP518 |
| B | HOH2506 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1562 |
| Chain | Residue |
| B | PHE256 |
| B | LEU257 |
| B | ASN388 |
| B | LYS394 |
| B | HOH2236 |
| B | HOH2350 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B1563 |
| Chain | Residue |
| A | TYR197 |
| A | PHE201 |
| B | ASP73 |
| B | ARG199 |
| B | LEU221 |
| B | PRO249 |
| B | HOH2229 |
| B | HOH2507 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B1564 |
| Chain | Residue |
| A | LYS179 |
| A | LEU181 |
| A | HOH2156 |
| B | ASP73 |
| B | PRO205 |
| B | ARG206 |
| B | ALA250 |
| B | SER251 |
| B | ASP252 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B1565 |
| Chain | Residue |
| B | GLU475 |
| B | GLN477 |
| B | GLU529 |
| B | ASN530 |
| B | HOH2470 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B1566 |
| Chain | Residue |
| A | TYR197 |
| B | GLU224 |
| B | MET225 |
| B | ASN226 |
| B | PRO227 |
| B | LYS228 |
| B | GLN245 |
| B | HOH2508 |
| B | HOH2509 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B1567 |
| Chain | Residue |
| B | GLN23 |
| B | GLY385 |
| B | SER386 |
| B | SOX1569 |
| site_id | BC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SOX B1569 |
| Chain | Residue |
| A | MET142 |
| A | PHE146 |
| B | SER1 |
| B | GLN23 |
| B | PHE24 |
| B | SER67 |
| B | ALA69 |
| B | PHE71 |
| B | ASN241 |
| B | ARG263 |
| B | ASN388 |
| B | EDO1567 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pnl |
| Chain | Residue | Details |
| B | ASN241 | |
| B | SER1 | |
| B | ALA69 | |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 841 |
| Chain | Residue | Details |
| B | SER1 | nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ALA69 | electrostatic stabiliser |
| B | ASN241 | electrostatic stabiliser |
