3N0G
Crystal Structure of Isoprene Synthase from Grey Poplar Leaves (Populus x canescens) in complex with three Mg2+ ions and dimethylallyl-S-thiolodiphosphate
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 | 0034009 | molecular_function | isoprene synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0120251 | biological_process | hydrocarbon biosynthetic process |
| 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 | 0034009 | molecular_function | isoprene synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0120251 | biological_process | hydrocarbon biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DST A 601 |
| Chain | Residue |
| A | ARG308 |
| A | ASN489 |
| A | MG621 |
| A | MG622 |
| A | MG623 |
| A | ASP345 |
| A | ASP349 |
| A | PHE420 |
| A | GLU423 |
| A | SER445 |
| A | SER446 |
| A | PHE485 |
| A | ARG486 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 621 |
| Chain | Residue |
| A | ASP345 |
| A | PHE420 |
| A | GLU423 |
| A | DST601 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 622 |
| Chain | Residue |
| A | GLU497 |
| A | ALA504 |
| A | DST601 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 623 |
| Chain | Residue |
| A | ASP345 |
| A | ASP349 |
| A | DST601 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DST B 612 |
| Chain | Residue |
| B | ARG308 |
| B | PHE338 |
| B | ASP345 |
| B | ASP349 |
| B | PHE420 |
| B | GLU423 |
| B | SER446 |
| B | PHE485 |
| B | ARG486 |
| B | ASN489 |
| B | MG631 |
| B | MG632 |
| B | MG633 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 631 |
| Chain | Residue |
| B | ASP345 |
| B | ASP349 |
| B | PHE420 |
| B | DST612 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 632 |
| Chain | Residue |
| B | DST612 |
| B | HOH727 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 633 |
| Chain | Residue |
| B | ASP345 |
| B | ASP349 |
| B | DST612 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20624401, ECO:0007744|PDB:3N0G |
| Chain | Residue | Details |
| A | ASP345 | |
| A | GLU497 | |
| B | ASP345 | |
| B | GLU497 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q40577 |
| Chain | Residue | Details |
| A | ASP349 | |
| A | ASN489 | |
| A | SER493 | |
| B | ASP349 | |
| B | ASN489 | |
| B | SER493 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:20624401, ECO:0007744|PDB:3N0G |
| Chain | Residue | Details |
| A | GLU423 | |
| A | ARG486 | |
| B | GLU423 | |
| B | ARG486 |
