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 | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0010333 | molecular_function | terpene synthase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| A | 0045483 | molecular_function | aristolochene synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0010333 | molecular_function | terpene synthase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| B | 0045483 | molecular_function | aristolochene synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008299 | biological_process | isoprenoid biosynthetic process |
| C | 0010333 | molecular_function | terpene synthase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| C | 0045483 | molecular_function | aristolochene synthase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008299 | biological_process | isoprenoid biosynthetic process |
| D | 0010333 | molecular_function | terpene synthase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| 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 | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17261032","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18385128","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17261032","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18385128","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BNX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18385128","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BNX","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 | PHE87 | |
| A | TRP308 | |
| A | TYR67 | |
| A | PHE153 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1di1 |
| Chain | Residue | Details |
| B | PHE87 | |
| B | TRP308 | |
| B | TYR67 | |
| B | PHE153 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1di1 |
| Chain | Residue | Details |
| C | PHE87 | |
| C | TRP308 | |
| C | TYR67 | |
| C | PHE153 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1di1 |
| Chain | Residue | Details |
| D | PHE87 | |
| D | TRP308 | |
| D | TYR67 | |
| D | PHE153 |
