6WKD
Crystal structure of pentalenene synthase complexed with 12,13-difluorofarnesyl diphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010333 | molecular_function | terpene synthase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050467 | molecular_function | pentalenene synthase activity |
| B | 0010333 | molecular_function | terpene synthase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050467 | molecular_function | pentalenene synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue FDF A 401 |
| Chain | Residue |
| A | PHE76 |
| A | SER223 |
| A | TRP308 |
| A | ARG314 |
| A | TYR315 |
| A | MG404 |
| A | HOH504 |
| A | HOH608 |
| A | PHE77 |
| A | ASP80 |
| A | TYR146 |
| A | TYR150 |
| A | ARG173 |
| A | ILE177 |
| A | THR182 |
| A | ASN219 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | PRO114 |
| A | HOH536 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASP80 |
| A | ASP84 |
| A | ARG314 |
| A | HOH504 |
| A | HOH641 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 404 |
| Chain | Residue |
| A | ASN219 |
| A | SER223 |
| A | FDF401 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | ARG14 |
| B | PRO59 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP80 | |
| A | ASP84 | |
| A | ASN219 | |
| B | ASP80 | |
| B | ASP84 | |
| B | ASN219 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER223 | |
| A | GLU227 | |
| B | SER223 | |
| B | GLU227 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 13 |
| Details | M-CSA 89 |
| Chain | Residue | Details |
| A | PHE76 | electrostatic stabiliser, van der waals interaction |
| A | GLU227 | metal ligand |
| A | ARG230 | electrostatic stabiliser |
| A | TRP308 | electrostatic stabiliser, van der waals interaction |
| A | HIS309 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | PHE77 | electrostatic stabiliser, steric role, van der waals interaction |
| A | ASP80 | metal ligand |
| A | ASP84 | metal ligand |
| A | ARG157 | electrostatic stabiliser |
| A | ARG173 | electrostatic stabiliser |
| A | ASN219 | electrostatic stabiliser, metal ligand, polar/non-polar interaction, steric role |
| A | SER223 | metal ligand |
| A | LYS226 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 13 |
| Details | M-CSA 89 |
| Chain | Residue | Details |
| B | PHE76 | electrostatic stabiliser, van der waals interaction |
| B | GLU227 | metal ligand |
| B | ARG230 | electrostatic stabiliser |
| B | TRP308 | electrostatic stabiliser, van der waals interaction |
| B | HIS309 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | PHE77 | electrostatic stabiliser, steric role, van der waals interaction |
| B | ASP80 | metal ligand |
| B | ASP84 | metal ligand |
| B | ARG157 | electrostatic stabiliser |
| B | ARG173 | electrostatic stabiliser |
| B | ASN219 | electrostatic stabiliser, metal ligand, polar/non-polar interaction, steric role |
| B | SER223 | metal ligand |
| B | LYS226 | electrostatic stabiliser |
