3MBM
Crystal structure of 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from Burkholderia pseudomallei with cytosine and FoL fragment 717, imidazo[2,1-b][1,3]thiazol-6-ylmethanol
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 | 717165 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CYT A 164 |
Chain | Residue |
A | LYS134 |
A | THR135 |
A | HOH198 |
A | HOH292 |
A | ALA102 |
A | PRO105 |
A | LYS106 |
A | LEU107 |
A | ALA108 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 717 A 165 |
Chain | Residue |
A | ASP10 |
A | HIS12 |
A | HIS44 |
A | PHE63 |
A | ASP65 |
A | ZN163 |
A | HOH257 |
A | HOH281 |
B | LYS134 |
B | GLU137 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TRS A 166 |
Chain | Residue |
A | TYR9 |
A | GLU149 |
A | GLN151 |
A | HOH169 |
A | HOH251 |
A | HOH272 |
B | TYR9 |
B | GLU149 |
B | GLN151 |
C | TYR9 |
C | GLU149 |
C | GLN151 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 163 |
Chain | Residue |
B | ASP10 |
B | HIS12 |
B | HIS44 |
B | 717165 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CYT B 164 |
Chain | Residue |
B | ALA102 |
B | PRO105 |
B | LYS106 |
B | LEU107 |
B | ALA108 |
B | ALA133 |
B | LYS134 |
B | THR135 |
B | HOH198 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 717 B 165 |
Chain | Residue |
B | ASP10 |
B | HIS12 |
B | HIS44 |
B | ZN163 |
B | HOH170 |
C | LYS134 |
C | GLU137 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 717 C 163 |
Chain | Residue |
A | LYS134 |
A | GLU137 |
C | ASP10 |
C | HIS12 |
C | HIS44 |
C | ILE59 |
C | PHE63 |
C | ZN164 |
C | HOH191 |
C | HOH202 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 164 |
Chain | Residue |
C | ASP10 |
C | HIS12 |
C | HIS44 |
C | 717163 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CYT C 165 |
Chain | Residue |
C | ALA102 |
C | PRO105 |
C | LYS106 |
C | LEU107 |
C | ALA108 |
C | ALA133 |
C | LYS134 |
C | THR135 |
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 | |
A | HIS44 | |
A | ASP58 | |
A | PHE63 | |
A | ARG144 | |
B | ASP10 | |
B | HIS12 | |
B | HIS36 | |
B | HIS44 | |
B | ASP58 | |
B | PHE63 | |
B | ARG144 | |
C | ASP10 | |
C | HIS12 | |
C | HIS36 | |
C | HIS44 | |
C | ASP58 | |
C | PHE63 | |
C | ARG144 | |
A | HIS12 | |
A | HIS36 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
B | ASP67 | |
B | ALA102 | |
B | ALA133 | |
C | ASP67 | |
C | ALA102 | |
C | ALA133 | |
A | ASP40 | |
B | ASP40 | |
C | ASP40 | |
A | ASP67 | |
A | ALA102 | |
A | ALA133 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00107 |
Chain | Residue | Details |
B | THR135 | |
C | HIS36 | |
C | THR135 | |
A | HIS36 | |
A | THR135 | |
B | HIS36 |