4C8E
IspF (Burkholderia cenocepacia) 2CMP complex
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 1162 |
| Chain | Residue |
| A | ASP10 |
| A | HIS12 |
| A | HIS44 |
| A | C5P1164 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1162 |
| Chain | Residue |
| B | ASP10 |
| B | HIS12 |
| B | HIS44 |
| B | C5P1164 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 1162 |
| Chain | Residue |
| C | HIS12 |
| C | HIS44 |
| C | C5P1165 |
| C | ASP10 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEG C 1163 |
| Chain | Residue |
| A | GLN151 |
| A | HOH2160 |
| A | HOH2167 |
| A | HOH2168 |
| B | LEU142 |
| B | GLU149 |
| B | HOH2011 |
| C | TYR9 |
| C | GLU149 |
| C | GLN151 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE C5P B 1163 |
| Chain | Residue |
| A | ASP58 |
| A | GLY60 |
| A | C5P1164 |
| A | HOH2020 |
| A | HOH2072 |
| A | HOH2175 |
| B | ALA102 |
| B | PRO105 |
| B | LYS106 |
| B | LEU107 |
| B | ALA108 |
| B | ALA133 |
| B | LYS134 |
| B | THR135 |
| B | HOH2082 |
| B | HOH2104 |
| B | HOH2116 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE C5P C 1164 |
| Chain | Residue |
| B | ASP58 |
| B | ILE59 |
| B | GLY60 |
| B | C5P1164 |
| B | HOH2013 |
| B | HOH2047 |
| B | HOH2117 |
| C | ALA102 |
| C | PRO105 |
| C | LYS106 |
| C | LEU107 |
| C | ALA108 |
| C | ALA133 |
| C | LYS134 |
| C | THR135 |
| C | HOH2109 |
| C | HOH2119 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE C5P A 1163 |
| Chain | Residue |
| A | ALA102 |
| A | PRO105 |
| A | LYS106 |
| A | LEU107 |
| A | ALA108 |
| A | ALA133 |
| A | LYS134 |
| A | THR135 |
| A | HOH2150 |
| A | HOH2152 |
| A | HOH2173 |
| C | ASP58 |
| C | GLY60 |
| C | C5P1165 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE C5P B 1164 |
| Chain | Residue |
| B | ASP10 |
| B | HIS12 |
| B | HIS36 |
| B | SER37 |
| B | HIS44 |
| B | ILE59 |
| B | GLY60 |
| B | ASP65 |
| B | ALA73 |
| B | LEU78 |
| B | ZN1162 |
| B | HOH2012 |
| B | HOH2032 |
| B | HOH2033 |
| B | HOH2056 |
| B | HOH2057 |
| B | HOH2117 |
| C | LYS134 |
| C | C5P1164 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE C5P A 1164 |
| Chain | Residue |
| A | ZN1162 |
| A | HOH2019 |
| A | HOH2056 |
| A | HOH2057 |
| A | HOH2175 |
| B | LYS134 |
| B | C5P1163 |
| A | ASP10 |
| A | HIS12 |
| A | HIS36 |
| A | SER37 |
| A | HIS44 |
| A | ILE59 |
| A | GLY60 |
| A | PHE63 |
| A | ALA73 |
| A | LEU78 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE C5P C 1165 |
| Chain | Residue |
| A | LYS134 |
| A | C5P1163 |
| A | HOH2154 |
| A | HOH2172 |
| C | ASP10 |
| C | HIS12 |
| C | HIS36 |
| C | SER37 |
| C | HIS44 |
| C | ILE59 |
| C | PHE63 |
| C | ALA73 |
| C | LEU78 |
| C | ZN1162 |
| C | HOH2039 |
| C | HOH2040 |
| C | HOH2041 |
| C | HOH2056 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1165 |
| Chain | Residue |
| A | HOH2163 |
| A | HOH2164 |
| B | GLY140 |
| B | TYR141 |
| B | ARG144 |
| B | ARG144 |
| B | HOH2118 |
| B | HOH2119 |
| C | GLY140 |
| C | ARG144 |
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 | 9 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP40 | |
| A | ALA102 | |
| A | ALA133 | |
| B | ASP40 | |
| B | ALA102 | |
| B | ALA133 | |
| C | ASP40 | |
| 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 |
