1TDC
STRUCTURES OF THYMIDYLATE SYNTHASE WITH A C-TERMINAL DELETION: ROLE OF THE C-TERMINUS IN ALIGNMENT OF D/UMP AND CH2H4FOLATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004799 | molecular_function | thymidylate synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006231 | biological_process | dTMP biosynthetic process |
| A | 0006235 | biological_process | dTTP biosynthetic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| A | 0032259 | biological_process | methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE UMP A 529 |
| Chain | Residue |
| A | ARG178 |
| A | HIS259 |
| A | TYR261 |
| A | ARG179 |
| A | GLN217 |
| A | ARG218 |
| A | SER219 |
| A | ALA220 |
| A | ASP221 |
| A | GLY225 |
| A | ASN229 |
Functional Information from PROSITE/UniProt
| site_id | PS00091 |
| Number of Residues | 29 |
| Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrlIvsaWNpedvptma.....LpPCHtlyQFyV |
| Chain | Residue | Details |
| A | ARG178-VAL206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00008","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00008","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00008","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| A | ASN229 | |
| A | CYS198 | |
| A | SER232 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| A | ASP221 | |
| A | HIS259 | |
| A | ASP257 | |
| A | GLU60 | |
| A | CYS198 | |
| A | SER219 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 31 |
| Chain | Residue | Details |
| A | GLU60 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | TRP82 | electrostatic stabiliser, hydrogen bond donor, van der waals interaction |
| A | TYR146 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | CYS198 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ARG218 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| A | ASP221 | activator, electrostatic stabiliser, hydrogen bond acceptor, steric role |
