3QHD
Crystal structure of 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE Synthase from BURKHOLDERIA PSEUDOMALLEI bound to CYTIDINE, FOL795 and FOL955
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 | MSR166 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 164 |
Chain | Residue |
A | HIS12 |
A | HIS36 |
A | SER37 |
A | HIS44 |
A | HOH210 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CTN A 165 |
Chain | Residue |
A | ALA102 |
A | PRO105 |
A | LYS106 |
A | LEU107 |
A | ALA108 |
A | ALA133 |
A | LYS134 |
A | HOH169 |
A | HOH211 |
A | HOH220 |
A | HOH248 |
A | HOH297 |
C | ASP58 |
C | GLY60 |
C | ARG61 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MSR A 166 |
Chain | Residue |
A | ASP10 |
A | HIS12 |
A | HIS44 |
A | PHE63 |
A | SER64 |
A | ASP65 |
A | PHE70 |
A | ZN163 |
B | LYS134 |
B | CTN165 |
B | HOH169 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 795 A 167 |
Chain | Residue |
A | HIS62 |
A | PHE63 |
A | ASP67 |
A | ARG69 |
A | ALA77 |
A | LEU78 |
A | ARG85 |
A | HOH327 |
B | ALA113 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K B 163 |
Chain | Residue |
A | HOH377 |
B | HOH378 |
C | HOH379 |
C | HOH380 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 164 |
Chain | Residue |
B | ASP10 |
B | HIS12 |
B | HIS44 |
C | HOH168 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CTN B 165 |
Chain | Residue |
A | ASP58 |
A | GLY60 |
A | MSR166 |
B | ALA102 |
B | PRO105 |
B | LYS106 |
B | LEU107 |
B | ALA108 |
B | ALA133 |
B | LYS134 |
B | THR135 |
B | HOH175 |
B | HOH176 |
B | HOH230 |
B | HOH307 |
B | HOH320 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 163 |
Chain | Residue |
A | HOH364 |
C | ASP10 |
C | HIS12 |
C | HIS44 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CTN C 165 |
Chain | Residue |
B | ASP58 |
B | GLY60 |
B | ARG61 |
C | ALA102 |
C | PRO105 |
C | LYS106 |
C | LEU107 |
C | ALA108 |
C | ALA133 |
C | LYS134 |
C | HOH297 |
C | HOH332 |
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 |