1EVF
CRYSTAL STRUCTURE ANALYSIS OF CYS167 MUTANT OF ESCHERICHIA COLI
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 320 |
| Chain | Residue |
| A | GLU223 |
| A | ARG225 |
| A | HIS255 |
| A | HOH421 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 321 |
| Chain | Residue |
| A | HOH572 |
| A | ARG21 |
| A | ARG126 |
| A | ARG127 |
| A | ARG166 |
| A | HOH381 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 322 |
| Chain | Residue |
| A | HIS51 |
| A | ARG53 |
| A | SER54 |
| A | HOH403 |
| A | HOH406 |
| A | HOH407 |
| A | HOH538 |
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 | 1 |
| 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 | CME146 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:8312270, ECO:0007744|PDB:1TYS |
| Chain | Residue | Details |
| A | HIS51 | |
| A | ASP169 | |
| A | ALA263 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC |
| Chain | Residue | Details |
| A | ARG126 |
