4GP2
Crystal structure of ISOPRENOID SYNTHASE A3MSH1 (TARGET EFI-501992) from pyrobaculum calidifontis complexed with DMAPP and Magnesium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004311 | molecular_function | geranylgeranyl diphosphate synthase activity |
| A | 0004659 | molecular_function | prenyltransferase activity |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0033386 | biological_process | geranylgeranyl diphosphate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004311 | molecular_function | geranylgeranyl diphosphate synthase activity |
| B | 0004659 | molecular_function | prenyltransferase activity |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0033386 | biological_process | geranylgeranyl diphosphate biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | ASP85 |
| A | ASP89 |
| A | MG402 |
| A | DMA403 |
| A | HOH561 |
| A | HOH591 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | DMA403 |
| A | HOH574 |
| A | HOH584 |
| A | HOH585 |
| A | ASP85 |
| A | ASP89 |
| A | MG401 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DMA A 403 |
| Chain | Residue |
| A | SER81 |
| A | LEU82 |
| A | ASP85 |
| A | ASP89 |
| A | ARG94 |
| A | LYS249 |
| A | MG401 |
| A | MG402 |
| A | DMA404 |
| A | HOH561 |
| A | HOH584 |
| A | HOH585 |
| A | HOH591 |
| A | HOH632 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DMA A 404 |
| Chain | Residue |
| A | GLY45 |
| A | LYS46 |
| A | ARG49 |
| A | HIS78 |
| A | ARG95 |
| A | THR185 |
| A | GLN222 |
| A | DMA403 |
| A | HOH507 |
| A | HOH510 |
| A | HOH546 |
| A | HOH586 |
| A | HOH613 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 405 |
| Chain | Residue |
| A | ASP225 |
| A | ASP229 |
| A | HOH543 |
| A | HOH575 |
| A | HOH582 |
| A | HOH594 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | ASP85 |
| B | ASP89 |
| B | MG402 |
| B | DMA404 |
| B | HOH565 |
| B | HOH566 |
| B | HOH567 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 402 |
| Chain | Residue |
| B | ASP85 |
| B | ASP89 |
| B | MG401 |
| B | DMA404 |
| B | HOH564 |
| B | HOH593 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 403 |
| Chain | Residue |
| B | ASP225 |
| B | ASP229 |
| B | HOH544 |
| B | HOH574 |
| B | HOH575 |
| B | HOH576 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DMA B 404 |
| Chain | Residue |
| B | SER81 |
| B | LEU82 |
| B | ASP85 |
| B | ASP89 |
| B | ARG94 |
| B | LYS184 |
| B | LYS243 |
| B | LYS249 |
| B | MG401 |
| B | MG402 |
| B | HOH564 |
| B | HOH566 |
| B | HOH567 |
| B | HOH593 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DMA B 405 |
| Chain | Residue |
| B | LYS46 |
| B | ARG49 |
| B | HIS78 |
| B | ARG95 |
| B | THR185 |
| B | PHE221 |
| B | HOH505 |
| B | HOH559 |
| B | HOH568 |
| B | HOH594 |
Functional Information from PROSITE/UniProt
| site_id | PS00723 |
| Number of Residues | 15 |
| Details | POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LIyDDii..DrgdvRRG |
| Chain | Residue | Details |
| A | LEU82-GLY96 |
