3RE3
Crystal Structure of 2-C-Methyl-D-Erythritol 2,4-Cyclodiphosphate Synthase from Francisella tularensis
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 |
| D | 0008299 | biological_process | isoprenoid biosynthetic process |
| D | 0008685 | molecular_function | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity |
| D | 0016114 | biological_process | terpenoid biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE POP A 163 |
| Chain | Residue |
| A | ASP10 |
| A | VAL11 |
| A | HIS12 |
| A | GLY40 |
| A | VAL42 |
| A | HIS45 |
| A | GLU138 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 165 |
| Chain | Residue |
| A | ALA54 |
| A | ASN96 |
| A | ILE97 |
| A | ASN131 |
| A | ARG4 |
| A | GLY53 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 160 |
| Chain | Residue |
| A | GLY141 |
| A | ARG145 |
| A | ARG145 |
| A | PO4161 |
| A | PO4161 |
| A | PO4161 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 161 |
| Chain | Residue |
| A | GLY141 |
| A | GLY141 |
| A | PHE142 |
| A | PHE142 |
| A | PHE142 |
| A | CL160 |
| A | CL160 |
| A | CL160 |
| A | HOH187 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE POP B 161 |
| Chain | Residue |
| B | ASP10 |
| B | VAL11 |
| B | HIS12 |
| B | ASP39 |
| B | GLY40 |
| B | VAL42 |
| B | HIS45 |
| B | HOH165 |
| C | THR136 |
| C | GLU138 |
| C | HOH171 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 160 |
| Chain | Residue |
| B | ASN96 |
| B | ILE97 |
| B | ASN131 |
| D | ARG4 |
| D | GLY53 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 C 162 |
| Chain | Residue |
| B | HIS152 |
| C | HIS152 |
| C | HOH170 |
| D | HIS152 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD C 163 |
| Chain | Residue |
| B | GLY141 |
| B | PHE142 |
| C | GLY141 |
| C | PHE142 |
| C | HOH169 |
| D | PHE142 |
| D | PO4162 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 161 |
| Chain | Residue |
| C | ARG4 |
| C | GLY53 |
| C | ALA54 |
| D | ASN96 |
| D | ILE97 |
| D | ASN131 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD C 160 |
| Chain | Residue |
| C | ASP10 |
| C | VAL11 |
| C | HIS45 |
| C | HOH166 |
| D | THR135 |
| D | THR136 |
| D | GLU138 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 D 162 |
| Chain | Residue |
| B | GLY141 |
| B | ARG145 |
| C | GLY141 |
| C | ARG145 |
| C | MPD163 |
| D | GLY141 |
| D | PHE142 |
| D | ARG145 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL D 160 |
| Chain | Residue |
| D | ASP10 |
Functional Information from PROSITE/UniProt
| site_id | PS01350 |
| Number of Residues | 16 |
| Details | ISPF 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase signature. SDGDVLiHAlcDAilG |
| Chain | Residue | Details |
| A | SER38-GLY53 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00107 |
| Chain | Residue | Details |
| A | ASP10 | |
| A | HIS37 | |
| A | HIS45 | |
| A | ASP59 | |
| A | PHE64 | |
| A | ALA103 | |
| A | THR135 | |
| A | PHE142 | |
| A | ARG145 | |
| B | ASP10 | |
| B | HIS12 | |
| B | HIS37 | |
| B | HIS45 | |
| B | ASP59 | |
| B | PHE64 | |
| B | ALA103 | |
| B | THR135 | |
| B | PHE142 | |
| B | ARG145 | |
| C | ASP10 | |
| C | HIS12 | |
| C | HIS37 | |
| C | HIS45 | |
| C | ASP59 | |
| C | PHE64 | |
| C | ALA103 | |
| C | THR135 | |
| C | PHE142 | |
| C | ARG145 | |
| D | ASP10 | |
| D | HIS12 | |
| D | HIS37 | |
| D | HIS45 | |
| D | ASP59 | |
| D | PHE64 | |
| D | ALA103 | |
| D | THR135 | |
| D | PHE142 | |
| D | ARG145 | |
| A | HIS12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00107 |
| Chain | Residue | Details |
| B | HIS37 | |
| B | THR136 | |
| C | HIS37 | |
| C | THR136 | |
| D | HIS37 | |
| D | THR136 | |
| A | HIS37 | |
| A | THR136 |
