1F4G
CRYSTAL STRUCTURE OF E. COLI THYMIDYLATE SYNTHASE COMPLEXED WITH SP-876
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 | 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 | 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 | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 703 |
Chain | Residue |
A | ARG21 |
A | ARG166 |
A | HOH761 |
A | HOH900 |
A | HOH907 |
A | HOH912 |
B | ARG126 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 704 |
Chain | Residue |
A | ARG53 |
A | HOH821 |
A | HOH827 |
A | HOH957 |
A | HIS51 |
A | LEU52 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 705 |
Chain | Residue |
A | GLU223 |
A | ARG225 |
A | HIS255 |
A | HOH732 |
A | HOH820 |
A | HOH1001 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 706 |
Chain | Residue |
A | ARG243 |
B | GLY106 |
B | ARG107 |
B | HIS108 |
site_id | AC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE TP4 A 601 |
Chain | Residue |
A | SER54 |
A | THR78 |
A | ILE79 |
A | TRP80 |
A | TRP83 |
A | LEU143 |
A | CYS146 |
A | SER167 |
A | ASP169 |
A | LEU172 |
A | GLY173 |
A | PHE176 |
A | ASN177 |
A | HIS207 |
A | TYR209 |
A | HOH711 |
A | HOH743 |
A | HOH777 |
A | HOH896 |
A | HOH898 |
A | HOH934 |
A | HOH954 |
A | HOH991 |
site_id | AC6 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE TP4 B 602 |
Chain | Residue |
B | HIS51 |
B | SER54 |
B | THR78 |
B | ILE79 |
B | TRP80 |
B | TRP83 |
B | CYS146 |
B | SER167 |
B | LEU172 |
B | GLY173 |
B | PHE176 |
B | ASN177 |
B | HIS207 |
B | TYR209 |
B | HOH718 |
B | HOH809 |
B | HOH814 |
B | HOH852 |
B | HOH853 |
B | HOH856 |
B | HOH887 |
B | HOH892 |
B | HOH910 |
B | HOH939 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 702 |
Chain | Residue |
A | ARG126 |
A | HOH926 |
A | HOH1014 |
B | ARG166 |
B | SER167 |
B | HOH834 |
Functional Information from PROSITE/UniProt
site_id | PS00091 |
Number of Residues | 29 |
Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriIvsaWNvgeldkma.....LaPCHaffQFyV |
Chain | Residue | Details |
A | ARG126-VAL154 |
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 | CYS146 | |
B | CYS146 |
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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1b02 |
Chain | Residue | Details |
A | HIS207 | |
A | GLU58 | |
A | ASP169 | |
A | SER167 | |
A | CYS146 | |
A | ASP205 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1b02 |
Chain | Residue | Details |
B | HIS207 | |
B | GLU58 | |
B | ASP169 | |
B | SER167 | |
B | CYS146 | |
B | ASP205 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b02 |
Chain | Residue | Details |
A | SER180 | |
A | ASN177 | |
A | CYS146 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b02 |
Chain | Residue | Details |
B | SER180 | |
B | ASN177 | |
B | CYS146 |