Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019350 | biological_process | teichoic acid biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047348 | molecular_function | glycerol-3-phosphate cytidylyltransferase activity |
| A | 0071555 | biological_process | cell wall organization |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019350 | biological_process | teichoic acid biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047348 | molecular_function | glycerol-3-phosphate cytidylyltransferase activity |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CTP A 130 |
| Chain | Residue |
| A | THR9 |
| A | ILE117 |
| A | SER118 |
| A | THR119 |
| A | THR120 |
| A | HOH1002 |
| A | HOH1042 |
| A | HOH1070 |
| A | PHE10 |
| A | HIS14 |
| A | HIS17 |
| A | LYS46 |
| A | GLY92 |
| A | ASP94 |
| A | ARG113 |
| A | THR114 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CTP B 630 |
| Chain | Residue |
| B | THR509 |
| B | PHE510 |
| B | HIS514 |
| B | HIS517 |
| B | LYS546 |
| B | GLY592 |
| B | ARG613 |
| B | THR614 |
| B | ILE617 |
| B | SER618 |
| B | THR619 |
| B | THR620 |
| B | HOH1003 |
| B | HOH1040 |
| B | HOH1050 |
| B | HOH1076 |
| B | HOH1080 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10508782","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14506262","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14506262","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 296 |
| Chain | Residue | Details |
| A | LYS44 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | LYS46 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 296 |
| Chain | Residue | Details |
| B | LYS544 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| B | LYS546 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
