1TDA
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 | 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 | 3 |
Details | BINDING SITE FOR RESIDUE PO4 A 317 |
Chain | Residue |
A | ARG179 |
A | ARG218 |
A | SER219 |
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 | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00008 |
Chain | Residue | Details |
A | CYS198 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00008 |
Chain | Residue | Details |
A | ARG23 | |
A | ARG218 | |
A | ASN229 | |
A | HIS259 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00008 |
Chain | Residue | Details |
A | ARG178 | |
A | ASP221 | |
A | ALA315 |
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 |