1F4D
CRYSTAL STRUCTURE OF E. COLI THYMIDYLATE SYNTHASE C146S, L143C COVALENTLY MODIFIED AT C143 WITH N-[TOSYL-D-PROLINYL]AMINO-ETHANETHIOL
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003723 | molecular_function | RNA binding |
| 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 | 0006417 | biological_process | regulation of translation |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0009314 | biological_process | response to radiation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| A | 0032259 | biological_process | methylation |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004799 | molecular_function | thymidylate synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006231 | biological_process | dTMP biosynthetic process |
| B | 0006235 | biological_process | dTTP biosynthetic process |
| B | 0006417 | biological_process | regulation of translation |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0009314 | biological_process | response to radiation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| B | 0032259 | biological_process | methylation |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 511 |
| Chain | Residue |
| A | HIS51 |
| A | LEU52 |
| A | ARG53 |
| A | HOH641 |
| A | HOH647 |
| A | HOH655 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 512 |
| Chain | Residue |
| A | HOH640 |
| A | GLU223 |
| A | ARG225 |
| A | HIS255 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 513 |
| Chain | Residue |
| B | HIS51 |
| B | LEU52 |
| B | ARG53 |
| B | HOH599 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 514 |
| Chain | Residue |
| A | ARG243 |
| B | ARG107 |
| B | HIS108 |
| B | HOH561 |
| B | HOH577 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TP2 A 401 |
| Chain | Residue |
| A | GLU58 |
| A | ILE79 |
| A | TRP80 |
| A | TRP83 |
| A | CYS143 |
| A | ASN177 |
| A | HOH525 |
| A | HOH579 |
| A | HOH598 |
| A | HOH673 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TP2 B 402 |
| Chain | Residue |
| B | GLU58 |
| B | ILE79 |
| B | TRP80 |
| B | TRP83 |
| B | CYS143 |
| B | ASN177 |
| B | HOH544 |
| B | HOH549 |
| B | HOH560 |
| B | HOH576 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | ARG21 |
| A | ARG166 |
| A | SER167 |
| A | HOH684 |
| B | ARG126 |
| B | ARG127 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| A | ARG126 |
| B | ARG21 |
| B | ARG166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00008, ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0000269|PubMed:9416600 |
| Chain | Residue | Details |
| A | SER146 | |
| B | SER146 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC |
| Chain | Residue | Details |
| A | ARG21 | |
| A | ARG166 | |
| A | ASN177 | |
| A | HIS207 | |
| B | ARG21 | |
| B | ARG166 | |
| B | ASN177 | |
| B | HIS207 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:8312270, ECO:0007744|PDB:1TYS |
| Chain | Residue | Details |
| A | HIS51 | |
| A | ASP169 | |
| A | ALA263 | |
| B | HIS51 | |
| B | ASP169 | |
| B | ALA263 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC |
| Chain | Residue | Details |
| A | ARG126 | |
| B | ARG126 |
