5HS2
Crystal structure of IspD complexed with CTP and Mg2+ from Bacillus subtilis at 1.90 Angstroms resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| A | 0050518 | molecular_function | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity |
| A | 0070567 | molecular_function | cytidylyltransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| B | 0050518 | molecular_function | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity |
| B | 0070567 | molecular_function | cytidylyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | binding site for residue CTP A 301 |
| Chain | Residue |
| A | PRO8 |
| A | LEU23 |
| A | GLY80 |
| A | ASP81 |
| A | GLU82 |
| A | ARG83 |
| A | SER86 |
| A | ASP104 |
| A | GLY105 |
| A | ALA106 |
| A | LYS209 |
| A | ALA9 |
| A | MG302 |
| A | HOH425 |
| A | HOH435 |
| A | HOH457 |
| A | HOH477 |
| A | HOH484 |
| A | HOH487 |
| A | HOH496 |
| A | HOH508 |
| A | HOH517 |
| A | ALA10 |
| A | GLY11 |
| A | GLN12 |
| A | GLY13 |
| A | LYS14 |
| A | ARG15 |
| A | LYS22 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | CTP301 |
| A | HOH484 |
| A | HOH496 |
| A | HOH508 |
Functional Information from PROSITE/UniProt
| site_id | PS01295 |
| Number of Residues | 8 |
| Details | ISPD 4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature. VLVHDGAR |
| Chain | Residue | Details |
| A | VAL100-ARG107 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG15 | |
| A | LYS22 | |
| B | ARG15 | |
| B | LYS22 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Positions MEP for the nucleophilic attack => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG152 | |
| A | LYS209 | |
| B | ARG152 | |
| B | LYS209 |
