1N24
(+)-Bornyl diphosphate synthase: Complex with Mg and product
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 | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 701 |
| Chain | Residue |
| A | ASP351 |
| A | ASP355 |
| A | MG703 |
| A | BP2801 |
| A | HOH883 |
| A | HOH884 |
| A | HOH885 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 702 |
| Chain | Residue |
| A | GLU504 |
| A | BP2801 |
| A | HOH880 |
| A | ASP496 |
| A | THR500 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 703 |
| Chain | Residue |
| A | ASP351 |
| A | ASP355 |
| A | MG701 |
| A | BP2801 |
| A | HOH881 |
| A | HOH882 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 704 |
| Chain | Residue |
| B | ASP351 |
| B | ASP355 |
| B | MG705 |
| B | BP2802 |
| B | HOH864 |
| B | HOH865 |
| B | HOH866 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 705 |
| Chain | Residue |
| B | ASP351 |
| B | ASP355 |
| B | MG704 |
| B | BP2802 |
| B | HOH862 |
| B | HOH863 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 706 |
| Chain | Residue |
| B | ASP496 |
| B | THR500 |
| B | BP2802 |
| B | HOH861 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE BP2 A 801 |
| Chain | Residue |
| A | ARG314 |
| A | THR348 |
| A | ASP351 |
| A | ASP355 |
| A | VAL452 |
| A | ARG493 |
| A | ASP496 |
| A | THR500 |
| A | GLU504 |
| A | LYS512 |
| A | TYR572 |
| A | PHE578 |
| A | MG701 |
| A | MG702 |
| A | MG703 |
| A | HOH879 |
| A | HOH880 |
| A | HOH881 |
| A | HOH883 |
| A | HOH891 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BP2 B 802 |
| Chain | Residue |
| B | ARG314 |
| B | THR348 |
| B | ASP351 |
| B | ASP355 |
| B | VAL452 |
| B | ARG493 |
| B | ASP496 |
| B | THR500 |
| B | LYS512 |
| B | TYR572 |
| B | PHE578 |
| B | MG704 |
| B | MG705 |
| B | MG706 |
| B | HOH861 |
| B | HOH862 |
| B | HOH863 |
| B | HOH864 |
| B | HOH865 |
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 |
