1N1B
Crystal Structure of (+)-Bornyl Diphosphate Synthase from Sage
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009507 | cellular_component | chloroplast |
| A | 0010333 | molecular_function | terpene synthase activity |
| A | 0016102 | biological_process | diterpenoid biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046211 | biological_process | (+)-camphor biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047926 | molecular_function | geranyl-diphosphate cyclase activity |
| A | 0102703 | molecular_function | camphene synthase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0009507 | cellular_component | chloroplast |
| B | 0010333 | molecular_function | terpene synthase activity |
| B | 0016102 | biological_process | diterpenoid biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046211 | biological_process | (+)-camphor biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047926 | molecular_function | geranyl-diphosphate cyclase activity |
| B | 0102703 | molecular_function | camphene synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 901 |
| Chain | Residue |
| B | ASP351 |
| B | ASP355 |
| B | HOH1006 |
| B | HOH1211 |
| B | HOH1212 |
| B | HOH1213 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 902 |
| Chain | Residue |
| A | HOH1173 |
| A | HOH1174 |
| A | HOH1175 |
| A | ASP351 |
| A | ASP355 |
| A | HOH1172 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG A 903 |
| Chain | Residue |
| A | TYR481 |
| A | ASP483 |
| A | CYS486 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG A 904 |
| Chain | Residue |
| A | PHE306 |
| A | VAL349 |
| A | CYS388 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE HG A 906 |
| Chain | Residue |
| A | CYS221 |
| A | HG907 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 907 |
| Chain | Residue |
| A | CYS221 |
| A | LEU222 |
| A | LYS225 |
| A | HG906 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 908 |
| Chain | Residue |
| A | CYS139 |
| A | GLU144 |
| A | VAL171 |
| A | CYS174 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG B 909 |
| Chain | Residue |
| B | TYR481 |
| B | ASP483 |
| B | CYS486 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE HG B 910 |
| Chain | Residue |
| B | TYR384 |
| B | CYS388 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG B 911 |
| Chain | Residue |
| B | PHE306 |
| B | VAL349 |
| B | CYS388 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG B 913 |
| Chain | Residue |
| B | ALA188 |
| B | CYS221 |
| B | HG914 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG B 914 |
| Chain | Residue |
| B | CYS221 |
| B | LEU222 |
| B | HG913 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 915 |
| Chain | Residue |
| B | CYS139 |
| B | GLU144 |
| B | VAL171 |
| B | CYS174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12432096, ECO:0007744|PDB:1N1Z |
| Chain | Residue | Details |
| A | ARG314 | |
| B | ASP351 | |
| B | ASP355 | |
| B | ARG493 | |
| B | ASP496 | |
| B | THR500 | |
| B | GLU504 | |
| B | LYS512 | |
| A | ASP351 | |
| A | ASP355 | |
| A | ARG493 | |
| A | ASP496 | |
| A | THR500 | |
| A | GLU504 | |
| A | LYS512 | |
| B | ARG314 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1n20 |
| Chain | Residue | Details |
| A | PHE578 | |
| A | TRP323 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1n20 |
| Chain | Residue | Details |
| B | PHE578 | |
| B | TRP323 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 259 |
| Chain | Residue | Details |
| A | TRP323 | electrostatic stabiliser, polar/non-polar interaction, steric role, van der waals interaction |
| A | ILE344 | steric role, van der waals interaction |
| A | ASP351 | metal ligand |
| A | ASP355 | metal ligand |
| A | VAL452 | steric role, van der waals interaction |
| A | ASP496 | metal ligand |
| A | THR500 | metal ligand |
| A | GLU504 | metal ligand |
| A | PHE578 | electrostatic stabiliser, polar/non-polar interaction, steric role, van der waals interaction |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 259 |
| Chain | Residue | Details |
| B | TRP323 | electrostatic stabiliser, polar/non-polar interaction, steric role, van der waals interaction |
| B | ILE344 | steric role, van der waals interaction |
| B | ASP351 | metal ligand |
| B | ASP355 | metal ligand |
| B | VAL452 | steric role, van der waals interaction |
| B | ASP496 | metal ligand |
| B | THR500 | metal ligand |
| B | GLU504 | metal ligand |
| B | PHE578 | electrostatic stabiliser, polar/non-polar interaction, steric role, van der waals interaction |
