1IPS
ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)
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 |
A | 1901362 | biological_process | organic cyclic compound biosynthetic process |
B | 0005506 | molecular_function | iron ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0009058 | biological_process | biosynthetic process |
B | 0016216 | molecular_function | isopenicillin-N synthase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0017000 | biological_process | antibiotic biosynthetic process |
B | 0031418 | molecular_function | L-ascorbic acid binding |
B | 0042318 | biological_process | penicillin biosynthetic process |
B | 0044283 | biological_process | small molecule biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 1901362 | biological_process | organic cyclic compound biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 350 |
Chain | Residue |
A | ASP216 |
A | HIS270 |
A | GLN330 |
A | HOH352 |
A | HOH353 |
A | HIS214 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN A 351 |
Chain | Residue |
A | GLU81 |
A | HIS82 |
A | HOH354 |
A | HOH355 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 350 |
Chain | Residue |
B | HIS214 |
B | ASP216 |
B | HIS270 |
B | GLN330 |
B | HOH352 |
B | HOH353 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MN B 351 |
Chain | Residue |
B | HIS82 |
B | HOH354 |
site_id | SA |
Number of Residues | 4 |
Details | ACTIVE SITE (MN BINDING), A CHAIN. |
Chain | Residue |
A | HIS214 |
A | ASP216 |
A | HIS270 |
A | GLN330 |
site_id | SB |
Number of Residues | 4 |
Details | ACTIVE SITE (MN BINDING), B CHAIN. |
Chain | Residue |
B | HIS214 |
B | ASP216 |
B | HIS270 |
B | GLN330 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:2BJS |
Chain | Residue | Details |
A | SER281 | |
B | ARG87 | |
B | TYR91 | |
B | TYR189 | |
B | ASP216 | |
B | SER281 | |
A | ARG87 | |
A | TYR91 | |
A | TYR189 | |
A | ASP216 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:2BJS |
Chain | Residue | Details |
A | SER183 | |
B | SER183 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1QJE |
Chain | Residue | Details |
A | HIS214 | |
B | HIS214 |
Chain | Residue | Details |
A | HIS270 | |
B | HIS270 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805 |
Chain | Residue | Details |
A | ARG279 | |
B | ARG279 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0007744|PDB:1QJE |
Chain | Residue | Details |
A | PHE211 | |
B | 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 |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 145 |
Chain | Residue | Details |
B | PHE211 | polar/non-polar interaction, steric role |
B | HIS214 | metal ligand |
B | ASP216 | metal ligand |
B | HIS270 | metal ligand |