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 |