1DGP
ARISTOLOCHENE SYNTHASE FARNESOL COMPLEX
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FOH A 401 |
| Chain | Residue |
| A | PHE112 |
| A | ARG200 |
| A | LYS206 |
| A | SER241 |
| A | ASN244 |
| A | ASP245 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FOH A 402 |
| Chain | Residue |
| A | PHE112 |
| A | PHE178 |
| A | GLY205 |
| A | LYS206 |
| A | LEU209 |
| A | LEU240 |
| A | ASN244 |
| A | TRP333 |
| A | VAL88 |
| A | TYR92 |
| A | LEU108 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FOH B 401 |
| Chain | Residue |
| B | PHE112 |
| B | ARG200 |
| B | LYS206 |
| B | SER241 |
| B | ASN244 |
| B | ASP245 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FOH B 402 |
| Chain | Residue |
| B | VAL88 |
| B | TYR92 |
| B | LEU108 |
| B | PHE112 |
| B | PHE178 |
| B | GLY205 |
| B | LYS206 |
| B | ASN244 |
| B | ASN330 |
| B | TRP333 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. LSIHELGHYL |
| Chain | Residue | Details |
| A | LEU188-LEU197 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9UR08","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"10825154","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DI1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1di1 |
| Chain | Residue | Details |
| A | TYR92 | |
| A | PHE112 | |
| A | TRP333 | |
| A | PHE178 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1di1 |
| Chain | Residue | Details |
| B | TYR92 | |
| B | PHE112 | |
| B | TRP333 | |
| B | PHE178 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 261 |
| Chain | Residue | Details |
| A | TYR92 | electrostatic stabiliser, steric role, van der waals interaction |
| A | PHE112 | electrostatic stabiliser, steric role, van der waals interaction |
| A | PHE178 | electrostatic stabiliser, steric role, van der waals interaction |
| A | LYS206 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | TRP333 | electrostatic stabiliser, steric role, van der waals interaction |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 261 |
| Chain | Residue | Details |
| B | TYR92 | electrostatic stabiliser, steric role, van der waals interaction |
| B | PHE112 | electrostatic stabiliser, steric role, van der waals interaction |
| B | PHE178 | electrostatic stabiliser, steric role, van der waals interaction |
| B | LYS206 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | TRP333 | electrostatic stabiliser, steric role, van der waals interaction |
