5B8F
X-ray Crystal Structure of a 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from Pseudomonas aeruginosa
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 | 3 |
| Details | binding site for residue MG A 201 |
| Chain | Residue |
| A | ASP8 |
| A | HIS10 |
| A | HIS42 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue C5P A 202 |
| Chain | Residue |
| A | THR132 |
| A | THR133 |
| A | HOH324 |
| A | HOH418 |
| A | HOH437 |
| A | HOH476 |
| B | ASP56 |
| A | ALA100 |
| A | PRO103 |
| A | LYS104 |
| A | MET105 |
| A | ALA106 |
| A | ALA131 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MPD A 203 |
| Chain | Residue |
| A | ARG67 |
| A | HOH307 |
| A | HOH308 |
| A | HOH322 |
| B | ARG67 |
| B | ALA75 |
| B | HOH313 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 201 |
| Chain | Residue |
| B | ASP8 |
| B | HIS10 |
| B | HIS42 |
| B | HOH491 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue C5P B 202 |
| Chain | Residue |
| B | ALA100 |
| B | PRO103 |
| B | MET105 |
| B | ALA106 |
| B | ALA131 |
| B | THR132 |
| B | THR133 |
| B | HOH304 |
| B | HOH305 |
| B | HOH308 |
| B | HOH321 |
| B | HOH503 |
| B | HOH504 |
| C | ASP56 |
| C | HOH329 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 B 203 |
| Chain | Residue |
| A | GLY138 |
| A | ARG142 |
| B | GLY138 |
| B | PHE139 |
| B | ARG142 |
| B | PO4206 |
| B | HOH390 |
| B | HOH403 |
| C | GLY138 |
| C | ARG142 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 204 |
| Chain | Residue |
| A | HIS149 |
| B | HIS149 |
| B | HOH405 |
| B | HOH423 |
| B | HOH447 |
| C | HIS149 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 B 205 |
| Chain | Residue |
| B | ARG157 |
| B | HOH440 |
| B | HOH507 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 206 |
| Chain | Residue |
| A | ARG142 |
| B | ARG142 |
| B | PO4203 |
| B | HOH331 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 201 |
| Chain | Residue |
| C | ALA-6 |
| C | ASP8 |
| C | HIS10 |
| C | HIS42 |
| site_id | AD2 |
| Number of Residues | 13 |
| Details | binding site for residue C5P C 202 |
| Chain | Residue |
| A | ASP56 |
| A | GLY58 |
| A | LYS59 |
| C | ALA100 |
| C | PRO103 |
| C | LYS104 |
| C | MET105 |
| C | ALA106 |
| C | ALA131 |
| C | THR132 |
| C | THR133 |
| C | HOH390 |
| C | HOH456 |
Functional Information from PROSITE/UniProt
| site_id | PS01350 |
| Number of Residues | 16 |
| Details | ISPF 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase signature. SDGDVLlHAlsDAllG |
| Chain | Residue | Details |
| A | SER35-GLY50 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00107 |
| Chain | Residue | Details |
| A | ASP8 | |
| A | ARG142 | |
| B | ASP8 | |
| B | HIS10 | |
| B | HIS34 | |
| B | HIS42 | |
| B | ASP56 | |
| B | PHE61 | |
| B | ALA100 | |
| B | THR132 | |
| B | PHE139 | |
| A | HIS10 | |
| B | ARG142 | |
| C | ASP8 | |
| C | HIS10 | |
| C | HIS34 | |
| C | HIS42 | |
| C | ASP56 | |
| C | PHE61 | |
| C | ALA100 | |
| C | THR132 | |
| C | PHE139 | |
| A | HIS34 | |
| C | ARG142 | |
| A | HIS42 | |
| A | ASP56 | |
| A | PHE61 | |
| A | ALA100 | |
| A | THR132 | |
| A | PHE139 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00107 |
| Chain | Residue | Details |
| A | HIS34 | |
| A | THR133 | |
| B | HIS34 | |
| B | THR133 | |
| C | HIS34 | |
| C | THR133 |
