1N22
(+)-Bornyl Diphosphate Synthase: Complex with Mg, pyrophosphate, and (4R)-7-aza-7,8-dihydrolimonene
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0009507 | cellular_component | chloroplast |
A | 0010333 | molecular_function | terpene synthase activity |
A | 0016102 | biological_process | diterpenoid biosynthetic process |
A | 0016114 | biological_process | terpenoid 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 | 0009507 | cellular_component | chloroplast |
B | 0010333 | molecular_function | terpene synthase activity |
B | 0016102 | biological_process | diterpenoid biosynthetic process |
B | 0016114 | biological_process | terpenoid 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 | MG702 |
A | POP901 |
A | HOH959 |
A | HOH960 |
A | HOH961 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 702 |
Chain | Residue |
A | MG701 |
A | POP901 |
A | HOH957 |
A | HOH958 |
A | ASP351 |
A | ASP355 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 703 |
Chain | Residue |
A | ASP496 |
A | THR500 |
A | GLU504 |
A | POP901 |
A | HOH955 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 704 |
Chain | Residue |
B | ASP351 |
B | ASP355 |
B | MG705 |
B | POP902 |
B | HOH953 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 705 |
Chain | Residue |
B | ASP351 |
B | ASP355 |
B | MG704 |
B | POP902 |
B | HOH949 |
B | HOH950 |
B | HOH951 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 706 |
Chain | Residue |
B | ASP496 |
B | GLU504 |
B | MG707 |
B | POP902 |
B | HOH952 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 707 |
Chain | Residue |
B | ASP496 |
B | SER501 |
B | MG706 |
B | POP902 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 7A8 A 801 |
Chain | Residue |
A | TRP323 |
A | ILE344 |
A | THR348 |
A | TYR426 |
A | VAL452 |
A | POP901 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 7A8 B 802 |
Chain | Residue |
B | TRP323 |
B | ILE344 |
B | THR348 |
B | ASP351 |
B | VAL452 |
B | LEU492 |
B | POP902 |
site_id | BC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE POP A 901 |
Chain | Residue |
A | ARG314 |
A | ASP351 |
A | ASP355 |
A | ARG493 |
A | ASP496 |
A | THR500 |
A | GLU504 |
A | LYS512 |
A | MG701 |
A | MG702 |
A | MG703 |
A | 7A8801 |
A | HOH955 |
A | HOH956 |
A | HOH957 |
A | HOH958 |
A | HOH960 |
A | HOH961 |
A | HOH985 |
site_id | BC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE POP B 902 |
Chain | Residue |
B | ARG314 |
B | ASP351 |
B | ASP355 |
B | ARG493 |
B | ASP496 |
B | SER501 |
B | GLU504 |
B | LYS512 |
B | MG704 |
B | MG705 |
B | MG706 |
B | MG707 |
B | 7A8802 |
B | HOH950 |
B | HOH951 |
B | HOH952 |
B | HOH953 |
B | HOH985 |
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 | 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 |
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 | 1 |
Details | Annotated By Reference To The Literature 1n20 |
Chain | Residue | Details |
B | TRP323 |