3M00
Crystal Structure of 5-epi-aristolochene synthase M4 mutant complexed with (2-cis,6-trans)-2-fluorofarnesyl diphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0010333 | molecular_function | terpene synthase activity |
| A | 0016102 | biological_process | diterpenoid biosynthetic process |
| A | 0016114 | biological_process | terpenoid biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051762 | biological_process | sesquiterpene biosynthetic process |
| A | 0102698 | molecular_function | 5-epi-aristolochene synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 2CF A 549 |
| Chain | Residue |
| A | ARG264 |
| A | ARG441 |
| A | ASP444 |
| A | TYR520 |
| A | MG550 |
| A | MG551 |
| A | MG552 |
| A | HOH553 |
| A | HOH554 |
| A | HOH556 |
| A | HOH563 |
| A | ILE297 |
| A | HOH565 |
| A | HOH566 |
| A | HOH836 |
| A | SER298 |
| A | ASP301 |
| A | ASP305 |
| A | THR401 |
| A | THR402 |
| A | THR403 |
| A | CYS440 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 550 |
| Chain | Residue |
| A | ASP444 |
| A | THR448 |
| A | GLU452 |
| A | 2CF549 |
| A | HOH554 |
| A | HOH555 |
| A | HOH556 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 551 |
| Chain | Residue |
| A | ASP301 |
| A | ASP305 |
| A | 2CF549 |
| A | MG552 |
| A | HOH562 |
| A | HOH563 |
| A | HOH566 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG A 552 |
| Chain | Residue |
| A | ASP301 |
| A | ASP305 |
| A | GLU379 |
| A | 2CF549 |
| A | MG551 |
| A | HOH564 |
| A | HOH565 |
| A | HOH566 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27328867 |
| Chain | Residue | Details |
| A | ARG264 | |
| A | ARG441 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9295271 |
| Chain | Residue | Details |
| A | ASP301 | |
| A | ASP305 | |
| A | ASP444 | |
| A | THR448 | |
| A | GLU452 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 265 |
| Chain | Residue | Details |
| A | ARG264 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
| A | TYR527 | electrostatic stabiliser, polar interaction |
| A | TRP273 | electrostatic stabiliser, hydrogen bond donor, polar interaction, proton acceptor, proton donor |
| A | THR401 | electrostatic stabiliser, polar interaction |
| A | THR402 | electrostatic stabiliser, polar interaction |
| A | THR403 | electrostatic stabiliser, polar interaction |
| A | ARG441 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
| A | ASP444 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | TYR520 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | ASP525 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
