3CKE
Crystal structure of aristolochene synthase in complex with 12,13-difluorofarnesyl 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 | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 701 |
| Chain | Residue |
| D | ASN219 |
| D | SER223 |
| D | GLU227 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG D 702 |
| Chain | Residue |
| D | ASP90 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 500 |
| Chain | Residue |
| A | ARG273 |
| D | THR255 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME D 1272 |
| Chain | Residue |
| D | ARG62 |
| D | CYS65 |
| C | PRO27 |
| C | GLU30 |
| D | CYS25 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FDF A 400 |
| Chain | Residue |
| A | TYR67 |
| A | PHE87 |
| A | ASP90 |
| A | PHE153 |
| A | LEU184 |
| A | ASN219 |
| A | ASN305 |
| A | TRP308 |
| A | ARG314 |
| A | TYR315 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FDF B 401 |
| Chain | Residue |
| B | TYR67 |
| B | ASP90 |
| B | PHE153 |
| B | LEU184 |
| B | ASN305 |
| B | ARG314 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FDF C 402 |
| Chain | Residue |
| C | LEU83 |
| C | PHE87 |
| C | ASP90 |
| C | PHE153 |
| C | GLN157 |
| C | GLY180 |
| C | LEU184 |
| C | ASN219 |
| C | ARG314 |
| C | TYR315 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE POP D 5963 |
| Chain | Residue |
| D | ASP90 |
| D | ASN219 |
| D | SER223 |
| D | GLU227 |
| D | ARG314 |
| D | TYR315 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 2647 |
| Chain | Residue |
| C | PHE60 |
| C | TRP308 |
| C | THR312 |
| C | ARG314 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17261032, ECO:0000269|PubMed:18385128 |
| Chain | Residue | Details |
| A | ASP90 | |
| B | ASP90 | |
| C | ASP90 | |
| D | ASP90 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17261032, ECO:0000269|PubMed:18385128, ECO:0007744|PDB:3BNX |
| Chain | Residue | Details |
| A | ASN219 | |
| D | ASN219 | |
| D | SER223 | |
| D | GLU227 | |
| A | SER223 | |
| A | GLU227 | |
| B | ASN219 | |
| B | SER223 | |
| B | GLU227 | |
| C | ASN219 | |
| C | SER223 | |
| C | GLU227 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18385128, ECO:0007744|PDB:3BNX |
| Chain | Residue | Details |
| A | ARG314 | |
| A | TYR315 | |
| B | ARG314 | |
| B | TYR315 | |
| C | ARG314 | |
| C | TYR315 | |
| D | ARG314 | |
| D | TYR315 |
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 |
