1HXA
CRYSTAL STRUCTURE OF TEAS W273S FORM 2
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 | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 851 |
| Chain | Residue |
| A | ASP444 |
| A | THR448 |
| A | GLU452 |
| A | HOH662 |
| A | HOH666 |
| A | FHP900 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 852 |
| Chain | Residue |
| A | HOH718 |
| A | HOH773 |
| A | ASP301 |
| A | ASP305 |
| A | GLU379 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 853 |
| Chain | Residue |
| A | GLU452 |
| A | GLN457 |
| A | HOH773 |
| A | FHP900 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FHP A 900 |
| Chain | Residue |
| A | GLU269 |
| A | PHE272 |
| A | SER273 |
| A | THR401 |
| A | THR402 |
| A | TYR404 |
| A | ARG441 |
| A | ASP444 |
| A | GLU452 |
| A | THR519 |
| A | TYR520 |
| A | TYR527 |
| A | LEU534 |
| A | HOH666 |
| A | HOH732 |
| A | MG851 |
| A | MG853 |
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 | CSA1 |
| Number of Residues | 10 |
| Details | Annotated By Reference To The Literature 5eat |
| Chain | Residue | Details |
| A | ARG441 | |
| A | THR402 | |
| A | THR401 | |
| A | THR403 | |
| A | TYR527 | |
| A | SER273 | |
| A | ARG264 | |
| A | ASP525 | |
| A | ASP444 | |
| A | TYR520 |
| 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 | SER273 | 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 |
