Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0009058 | biological_process | biosynthetic process |
A | 0016216 | molecular_function | isopenicillin-N synthase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0017000 | biological_process | antibiotic biosynthetic process |
A | 0031418 | molecular_function | L-ascorbic acid binding |
A | 0042318 | biological_process | penicillin biosynthetic process |
A | 0044283 | biological_process | small molecule biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 401 |
Chain | Residue |
A | ARG27 |
A | HOH529 |
A | HOH533 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 402 |
Chain | Residue |
A | ARG37 |
A | LYS208 |
A | LYS266 |
A | ARG300 |
site_id | AC3 |
Number of Residues | 18 |
Details | binding site for residue ACV A 403 |
Chain | Residue |
A | SER183 |
A | ILE187 |
A | TYR189 |
A | PHE211 |
A | HIS214 |
A | ASP216 |
A | VAL272 |
A | SER281 |
A | PHE285 |
A | OXY404 |
A | FE405 |
A | HOH532 |
A | HOH534 |
A | HOH549 |
A | HOH625 |
A | HOH695 |
A | ARG87 |
A | TYR91 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue OXY A 404 |
Chain | Residue |
A | HIS214 |
A | HIS270 |
A | ACV403 |
A | FE405 |
A | HOH625 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue FE A 405 |
Chain | Residue |
A | HIS214 |
A | ASP216 |
A | HIS270 |
A | ACV403 |
A | OXY404 |
A | HOH625 |
Functional Information from PROSITE/UniProt
site_id | PS00185 |
Number of Residues | 10 |
Details | IPNS_1 Isopenicillin N synthase signature 1. KkAveSfCYL |
Chain | Residue | Details |
A | LYS97-LEU106 | |
site_id | PS00186 |
Number of Residues | 14 |
Details | IPNS_2 Isopenicillin N synthase signature 2. LInCGSymAhlTnN |
Chain | Residue | Details |
A | LEU250-ASN263 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ARG87 | |
A | TYR91 | |
A | TYR189 | |
A | ASP216 | |
A | SER281 | |
Chain | Residue | Details |
A | SER183 | |
Chain | Residue | Details |
A | HIS214 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ, ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2, ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4, ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1, ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN, ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:1QJF, ECO:0007744|PDB:1UZW, ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04, ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06, ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X, ECO:0007744|PDB:2BU9, ECO:0007744|PDB:2IVI, ECO:0007744|PDB:2IVJ, ECO:0007744|PDB:2JB4, ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB, ECO:0007744|PDB:2VBD, ECO:0007744|PDB:2VBP, ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1, ECO:0007744|PDB:2WO7, ECO:0007744|PDB:2Y60, ECO:0007744|PDB:2Y6F, ECO:0007744|PDB:3ZKU, ECO:0007744|PDB:3ZOI, ECO:0007744|PDB:4BB3 |
Chain | Residue | Details |
A | HIS270 | |
Chain | Residue | Details |
A | ARG279 | |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0007744|PDB:1QJE |
Chain | Residue | Details |
A | PHE211 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 145 |
Chain | Residue | Details |
A | PHE211 | polar/non-polar interaction, steric role |
A | HIS214 | metal ligand |
A | ASP216 | metal ligand |
A | HIS270 | metal ligand |