5NX5
Crystal structure of Linalool/Nerolidol synthase from Streptomyces clavuligerus in complex with 2-fluorogeranyl diphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0010333 | molecular_function | terpene synthase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0033383 | biological_process | geranyl diphosphate metabolic process |
| A | 0034008 | molecular_function | R-linalool synthase activity |
| A | 0045338 | biological_process | farnesyl diphosphate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0010333 | molecular_function | terpene synthase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0033383 | biological_process | geranyl diphosphate metabolic process |
| B | 0034008 | molecular_function | R-linalool synthase activity |
| B | 0045338 | biological_process | farnesyl diphosphate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASP80 |
| A | 0FV402 |
| A | HOH509 |
| A | HOH525 |
| A | HOH632 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue 0FV A 402 |
| Chain | Residue |
| A | ASP83 |
| A | ARG172 |
| A | VAL214 |
| A | ASN218 |
| A | LYS225 |
| A | MG401 |
| A | HOH509 |
| A | HOH520 |
| A | LEU72 |
| A | PHE76 |
| A | ASP79 |
| A | ASP80 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | ARG195 |
| A | ARG196 |
| A | HOH668 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | ASP164 |
| A | ALA166 |
| A | ALA167 |
| A | ARG170 |
| A | HOH507 |
| A | HOH636 |
| B | PHE208 |
| B | SER263 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | PRO151 |
| B | ARG196 |
| B | HIS199 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 401 |
| Chain | Residue |
| B | ARG172 |
| B | ASN218 |
| B | SER222 |
| B | LYS225 |
| B | ARG308 |
| B | TYR309 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 402 |
| Chain | Residue |
| B | ARG195 |
| B | ARG196 |
| B | HOH613 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| A | SER263 |
| B | ASP164 |
| B | ALA166 |
| B | ALA167 |
| B | ARG170 |
| B | HOH550 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| A | ARG195 |
| A | HIS199 |
| B | LEU93 |
| B | PRO151 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 405 |
| Chain | Residue |
| A | ARG202 |
| A | LEU267 |
| B | HIS159 |
| B | LEU163 |
| B | ASP164 |
| B | ALA167 |
| B | HOH550 |
| B | HOH575 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28966840, ECO:0007744|PDB:5NX5 |
| Chain | Residue | Details |
| B | ASP79 | |
| B | LYS225 | |
| A | ASP79 | |
| A | LYS225 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:B5GMG2 |
| Chain | Residue | Details |
| B | ASN218 | |
| B | SER222 | |
| B | ASP226 | |
| B | ARG308 | |
| A | ARG172 | |
| A | ASN218 | |
| A | SER222 | |
| A | ASP226 | |
| A | ARG308 | |
| B | ARG172 |
