2E4O
X-ray Crystal Structure of Aristolochene Synthase from Aspergillus terreus and the Evolution of Templates for the Cyclization of Farnesyl Diphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010333 | molecular_function | terpene synthase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0045483 | molecular_function | aristolochene synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0010333 | molecular_function | terpene synthase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0045483 | molecular_function | aristolochene synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0010333 | molecular_function | terpene synthase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0044281 | biological_process | small molecule metabolic process |
| C | 0045483 | molecular_function | aristolochene synthase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0010333 | molecular_function | terpene synthase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0044281 | biological_process | small molecule metabolic process |
| D | 0045483 | molecular_function | aristolochene synthase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 506 |
| Chain | Residue |
| B | ARG314 |
| B | TYR315 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 507 |
| Chain | Residue |
| C | ARG314 |
| C | TYR315 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES D 4246 |
| Chain | Residue |
| D | TYR315 |
| D | PHE87 |
| D | PHE153 |
| D | ASN219 |
| D | TRP308 |
| D | ARG314 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME D 500 |
| Chain | Residue |
| C | GLU30 |
| C | HOH536 |
| D | CYS25 |
| D | ARG62 |
| D | CYS65 |
| D | LEU66 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME A 501 |
| Chain | Residue |
| A | CYS25 |
| A | ARG62 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME C 502 |
| Chain | Residue |
| C | MET166 |
| C | CYS242 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 503 |
| Chain | Residue |
| A | ALA163 |
| A | ARG164 |
| A | MET166 |
| A | CYS242 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME C 504 |
| Chain | Residue |
| C | CYS25 |
| C | ARG62 |
| D | GLU30 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17261032, ECO:0000269|PubMed:18385128 |
| Chain | Residue | Details |
| A | ASP90 | |
| B | ASP90 | |
| B | ASN219 | |
| B | SER223 | |
| B | GLU227 | |
| C | ASP90 | |
| C | ASN219 | |
| C | SER223 | |
| C | GLU227 | |
| D | ASP90 | |
| D | ASN219 | |
| D | SER223 | |
| D | GLU227 | |
| A | ASN219 | |
| A | SER223 | |
| A | GLU227 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18385128 |
| Chain | Residue | Details |
| A | ARG175 | |
| A | LYS226 | |
| B | ARG175 | |
| B | LYS226 | |
| C | ARG175 | |
| C | LYS226 | |
| D | ARG175 | |
| D | LYS226 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG314 | |
| B | ARG314 | |
| C | ARG314 | |
| D | ARG314 |
