6XHT
Crystal structure of S. aureus TarI in complex with CDP-ribitol (space group P1211)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0047349 | molecular_function | D-ribitol-5-phosphate cytidylyltransferase activity |
| A | 0050518 | molecular_function | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity |
| A | 0070567 | molecular_function | cytidylyltransferase activity |
| A | 1902012 | biological_process | poly(ribitol phosphate) teichoic acid biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0047349 | molecular_function | D-ribitol-5-phosphate cytidylyltransferase activity |
| B | 0050518 | molecular_function | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity |
| B | 0070567 | molecular_function | cytidylyltransferase activity |
| B | 1902012 | biological_process | poly(ribitol phosphate) teichoic acid biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0008299 | biological_process | isoprenoid biosynthetic process |
| C | 0047349 | molecular_function | D-ribitol-5-phosphate cytidylyltransferase activity |
| C | 0050518 | molecular_function | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity |
| C | 0070567 | molecular_function | cytidylyltransferase activity |
| C | 1902012 | biological_process | poly(ribitol phosphate) teichoic acid biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0008299 | biological_process | isoprenoid biosynthetic process |
| D | 0047349 | molecular_function | D-ribitol-5-phosphate cytidylyltransferase activity |
| D | 0050518 | molecular_function | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity |
| D | 0070567 | molecular_function | cytidylyltransferase activity |
| D | 1902012 | biological_process | poly(ribitol phosphate) teichoic acid biosynthetic process |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0008299 | biological_process | isoprenoid biosynthetic process |
| E | 0047349 | molecular_function | D-ribitol-5-phosphate cytidylyltransferase activity |
| E | 0050518 | molecular_function | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity |
| E | 0070567 | molecular_function | cytidylyltransferase activity |
| E | 1902012 | biological_process | poly(ribitol phosphate) teichoic acid biosynthetic process |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0008299 | biological_process | isoprenoid biosynthetic process |
| F | 0047349 | molecular_function | D-ribitol-5-phosphate cytidylyltransferase activity |
| F | 0050518 | molecular_function | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity |
| F | 0070567 | molecular_function | cytidylyltransferase activity |
| F | 1902012 | biological_process | poly(ribitol phosphate) teichoic acid biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue SCN A 301 |
| Chain | Residue |
| A | LEU7 |
| A | GLY10 |
| A | GLN23 |
| A | ASP111 |
| A | ALA112 |
| A | VAL113 |
| A | HOH543 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SCN A 302 |
| Chain | Residue |
| A | LYS22 |
| A | HOH453 |
| D | LYS123 |
| A | LEU20 |
| A | PRO21 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue V2V B 301 |
| Chain | Residue |
| A | ASP143 |
| A | THR144 |
| A | ARG160 |
| B | LEU7 |
| B | ALA8 |
| B | GLY9 |
| B | GLY10 |
| B | GLY81 |
| B | SER82 |
| B | ASP83 |
| B | ARG84 |
| B | THR87 |
| B | ASP111 |
| B | ALA112 |
| B | VAL113 |
| B | ARG114 |
| B | GLY166 |
| B | GLN167 |
| B | GLN170 |
| B | SER193 |
| B | LYS217 |
| B | THR219 |
| B | HOH422 |
| B | HOH435 |
| B | HOH448 |
| B | HOH463 |
| B | HOH503 |
| B | HOH504 |
| B | HOH533 |
| B | HOH537 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SCN B 302 |
| Chain | Residue |
| B | PHE24 |
| B | HIS60 |
| B | THR64 |
| B | HOH489 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SCN B 303 |
| Chain | Residue |
| B | LYS48 |
| B | HIS94 |
| B | THR98 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SCN C 301 |
| Chain | Residue |
| C | LEU7 |
| C | GLY10 |
| C | GLN23 |
| C | ALA112 |
| C | VAL113 |
| C | HOH475 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue SCN C 302 |
| Chain | Residue |
| C | PRO21 |
| C | LYS22 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SCN D 301 |
| Chain | Residue |
| D | LEU7 |
| D | GLY10 |
| D | GLN23 |
| D | ASP111 |
| D | ALA112 |
| D | VAL113 |
| D | HOH479 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue SCN D 302 |
| Chain | Residue |
| D | PRO21 |
| D | LYS22 |
| site_id | AD1 |
| Number of Residues | 29 |
| Details | binding site for residue V2V E 301 |
| Chain | Residue |
| E | LEU7 |
| E | ALA8 |
| E | GLY9 |
| E | GLY10 |
| E | GLY81 |
| E | SER82 |
| E | ASP83 |
| E | ARG84 |
| E | THR87 |
| E | ASP111 |
| E | ALA112 |
| E | VAL113 |
| E | ARG114 |
| E | GLY166 |
| E | GLN167 |
| E | GLN170 |
| E | SER193 |
| E | LYS217 |
| E | HOH410 |
| E | HOH415 |
| E | HOH433 |
| E | HOH435 |
| E | HOH449 |
| E | HOH456 |
| E | HOH458 |
| E | HOH486 |
| F | ASP143 |
| F | THR144 |
| F | ARG160 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue SCN E 302 |
| Chain | Residue |
| E | HOH507 |
| E | PHE24 |
| E | PRO31 |
| E | HIS60 |
| E | THR64 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue SCN F 301 |
| Chain | Residue |
| F | LEU7 |
| F | GLY10 |
| F | GLN23 |
| F | ASP111 |
| F | ALA112 |
| F | VAL113 |
| F | HOH490 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SCN F 302 |
| Chain | Residue |
| F | PRO21 |
| F | LYS22 |
| F | HOH492 |
Functional Information from PROSITE/UniProt
| site_id | PS01295 |
| Number of Residues | 8 |
| Details | ISPD 4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature. IVTHDAVR |
| Chain | Residue | Details |
| A | ILE107-ARG114 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 54 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02068","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_02068","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Site: {"description":"Positions ribitol 5-phosphate for the nucleophilic attack","evidences":[{"source":"HAMAP-Rule","id":"MF_02068","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






