3KE1
Crystal structure of 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from Burkholderia pseudomallei in complex with a fragment-nucleoside fusion D000161829
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0008685 | molecular_function | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity |
| A | 0016114 | biological_process | terpenoid biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0008685 | molecular_function | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity |
| B | 0016114 | biological_process | terpenoid biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008299 | biological_process | isoprenoid biosynthetic process |
| C | 0008685 | molecular_function | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity |
| C | 0016114 | biological_process | terpenoid biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 163 |
| Chain | Residue |
| A | ASP10 |
| A | HIS12 |
| A | HIS44 |
| A | 829164 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 829 A 164 |
| Chain | Residue |
| A | GLY60 |
| A | ZN163 |
| A | HOH197 |
| A | HOH216 |
| B | ALA102 |
| B | PRO105 |
| B | LYS106 |
| B | LEU107 |
| B | ALA108 |
| B | ALA133 |
| B | LYS134 |
| B | THR135 |
| A | ASP10 |
| A | HIS12 |
| A | HIS44 |
| A | ASP58 |
| A | ILE59 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K A 165 |
| Chain | Residue |
| A | HOH209 |
| B | HOH191 |
| C | HOH195 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 163 |
| Chain | Residue |
| B | ASP10 |
| B | HIS12 |
| B | HIS44 |
| B | 829164 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 829 B 164 |
| Chain | Residue |
| B | ASP10 |
| B | HIS12 |
| B | HIS44 |
| B | ASP58 |
| B | GLY60 |
| B | ZN163 |
| C | ALA102 |
| C | PRO105 |
| C | LEU107 |
| C | ALA108 |
| C | ALA133 |
| C | LYS134 |
| C | THR135 |
| C | GLU137 |
| C | HOH171 |
| C | HOH202 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 163 |
| Chain | Residue |
| C | ASP10 |
| C | HIS12 |
| C | HIS44 |
| C | 829164 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 829 C 164 |
| Chain | Residue |
| A | ALA102 |
| A | PRO105 |
| A | LYS106 |
| A | LEU107 |
| A | ALA108 |
| A | ALA133 |
| A | LYS134 |
| A | THR135 |
| A | GLU137 |
| A | HOH220 |
| C | ASP10 |
| C | HIS12 |
| C | HIS44 |
| C | ASP58 |
| C | GLY60 |
| C | ZN163 |
Functional Information from PROSITE/UniProt
| site_id | PS01350 |
| Number of Residues | 16 |
| Details | ISPF 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase signature. SDADVLlHAitDAlfG |
| Chain | Residue | Details |
| A | SER37-GLY52 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00107 |
| Chain | Residue | Details |
| A | ASP10 | |
| B | HIS36 | |
| B | HIS44 | |
| B | ASP58 | |
| B | PHE63 | |
| B | ARG144 | |
| C | ASP10 | |
| C | HIS12 | |
| C | HIS36 | |
| C | HIS44 | |
| C | ASP58 | |
| A | HIS12 | |
| C | PHE63 | |
| C | ARG144 | |
| A | HIS36 | |
| A | HIS44 | |
| A | ASP58 | |
| A | PHE63 | |
| A | ARG144 | |
| B | ASP10 | |
| B | HIS12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP67 | |
| A | ASP40 | |
| B | ASP40 | |
| C | ASP40 | |
| A | ALA102 | |
| A | ALA133 | |
| B | ASP67 | |
| B | ALA102 | |
| B | ALA133 | |
| C | ASP67 | |
| C | ALA102 | |
| C | ALA133 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00107 |
| Chain | Residue | Details |
| A | HIS36 | |
| A | THR135 | |
| B | HIS36 | |
| B | THR135 | |
| C | HIS36 | |
| C | THR135 |
