3N2I
2.25 Angstrom resolution crystal structure of a thymidylate kinase (tmk) from Vibrio cholerae O1 biovar eltor str. N16961 in complex with thymidine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| A | 0004798 | molecular_function | dTMP kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006227 | biological_process | dUDP biosynthetic process |
| A | 0006233 | biological_process | dTDP biosynthetic process |
| A | 0006235 | biological_process | dTTP biosynthetic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| B | 0004798 | molecular_function | dTMP kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006227 | biological_process | dUDP biosynthetic process |
| B | 0006233 | biological_process | dTDP biosynthetic process |
| B | 0006235 | biological_process | dTTP biosynthetic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 213 |
| Chain | Residue |
| A | GLY13 |
| A | ALA14 |
| A | GLY15 |
| A | LYS16 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE THM A 214 |
| Chain | Residue |
| A | SER102 |
| A | SER103 |
| A | TYR106 |
| A | GLN107 |
| A | ILE157 |
| A | HOH249 |
| A | GLU12 |
| A | GLU40 |
| A | PRO41 |
| A | ARG51 |
| A | ARG76 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 213 |
| Chain | Residue |
| B | GLY13 |
| B | ALA14 |
| B | GLY15 |
| B | LYS16 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE THM B 214 |
| Chain | Residue |
| B | GLU40 |
| B | PRO41 |
| B | ARG51 |
| B | VAL72 |
| B | ARG76 |
| B | ARG98 |
| B | SER102 |
| B | SER103 |
| B | TYR106 |
| B | GLN107 |
| B | ASP155 |
Functional Information from PROSITE/UniProt
| site_id | PS01331 |
| Number of Residues | 13 |
| Details | THYMIDYLATE_KINASE Thymidylate kinase signature. VGDRHdmSSqAYQ |
| Chain | Residue | Details |
| A | VAL95-GLN107 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
