1GTV
CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE-5'-DIPHOSPHATE (TDP)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004798 | molecular_function | dTMP kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005525 | molecular_function | GTP 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 |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046044 | biological_process | TMP metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004798 | molecular_function | dTMP kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005525 | molecular_function | GTP 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 |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046044 | biological_process | TMP metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | ASP9 |
| A | GLU166 |
| A | TYD302 |
| A | HOH2193 |
| A | HOH2244 |
| B | ASP9 |
| B | GLU166 |
| B | TMP302 |
| B | HOH2029 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | GLY10 |
| A | ALA11 |
| A | GLY12 |
| A | LYS13 |
| A | ARG14 |
| A | ARG153 |
| B | GLY10 |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
| B | ARG14 |
| B | ARG153 |
| B | SO4303 |
| B | HOH2017 |
| B | HOH2019 |
| B | HOH2031 |
| B | HOH2032 |
| B | HOH2033 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SO4 A 304 |
| Chain | Residue |
| A | GLN121 |
| A | LYS132 |
| A | ALA154 |
| A | ALA161 |
| A | ARG162 |
| A | ARG167 |
| A | TRP187 |
| A | GLY188 |
| B | GLN121 |
| B | LYS132 |
| B | ALA154 |
| B | ARG162 |
| B | ARG167 |
| B | TRP187 |
| B | GLY188 |
| B | SO4304 |
| B | HOH2034 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 305 |
| Chain | Residue |
| A | TYR39 |
| A | ALA49 |
| A | HIS53 |
| A | TYD302 |
| B | TYR39 |
| B | ALA49 |
| B | HIS53 |
| B | ACT305 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SO4 A 306 |
| Chain | Residue |
| A | GLU55 |
| A | GLU55 |
| A | HIS56 |
| A | TRP119 |
| A | ARG122 |
| A | ILE123 |
| A | ARG127 |
| A | HOH2078 |
| A | HOH2249 |
| B | GLU55 |
| B | GLU55 |
| B | HIS56 |
| B | TRP119 |
| B | ARG122 |
| B | ILE123 |
| B | ARG127 |
| B | SO4306 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 307 |
| Chain | Residue |
| A | ASP46 |
| A | ARG127 |
| A | HOH2250 |
| B | ASP46 |
| B | ARG127 |
| B | ACT307 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 308 |
| Chain | Residue |
| A | ARG25 |
| A | SER30 |
| A | VAL31 |
| B | ARG25 |
| B | SER30 |
| B | VAL31 |
| B | ACT308 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MG B 301 |
| Chain | Residue |
| A | ASP9 |
| A | GLU166 |
| A | TYD302 |
| A | HOH2193 |
| A | HOH2244 |
| B | ASP9 |
| B | GLU166 |
| B | TMP302 |
| B | HOH2029 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SO4 B 303 |
| Chain | Residue |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
| B | ARG14 |
| B | ARG153 |
| B | HOH2017 |
| B | HOH2019 |
| B | HOH2031 |
| B | HOH2032 |
| B | HOH2033 |
| A | GLY10 |
| A | ALA11 |
| A | GLY12 |
| A | LYS13 |
| A | ARG14 |
| A | ARG153 |
| A | SO4303 |
| B | GLY10 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SO4 B 304 |
| Chain | Residue |
| A | GLN121 |
| A | LYS132 |
| A | ALA154 |
| A | ALA161 |
| A | ARG162 |
| A | ARG167 |
| A | TRP187 |
| A | GLY188 |
| A | SO4304 |
| B | GLN121 |
| B | LYS132 |
| B | ALA154 |
| B | ALA161 |
| B | ARG162 |
| B | ARG167 |
| B | TRP187 |
| B | GLY188 |
| B | HOH2034 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 305 |
| Chain | Residue |
| A | TYR39 |
| A | TYD302 |
| A | ACT305 |
| B | HOH2010 |
| B | HOH2011 |
| site_id | BC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SO4 B 306 |
| Chain | Residue |
| A | GLU55 |
| A | GLU55 |
| A | HIS56 |
| A | TRP119 |
| A | ARG122 |
| A | ILE123 |
| A | ARG127 |
| A | SO4306 |
| A | HOH2078 |
| A | HOH2249 |
| B | GLU55 |
| B | GLU55 |
| B | HIS56 |
| B | TRP119 |
| B | ARG122 |
| B | ILE123 |
| B | ARG127 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 307 |
| Chain | Residue |
| A | ASP46 |
| A | ARG127 |
| A | ACT307 |
| A | HOH2250 |
| B | ASP46 |
| B | ARG127 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT B 308 |
| Chain | Residue |
| A | ARG25 |
| A | SER30 |
| A | VAL31 |
| A | ACT308 |
| B | ARG25 |
| B | SER30 |
| B | VAL31 |
| site_id | BC6 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE TYD A 302 |
| Chain | Residue |
| A | ASP9 |
| A | PRO37 |
| A | TYR39 |
| A | PHE70 |
| A | ARG74 |
| A | ARG95 |
| A | ASN100 |
| A | TYR103 |
| A | TYR165 |
| A | GLU166 |
| A | MG301 |
| A | ACT305 |
| A | HOH2193 |
| A | HOH2243 |
| A | HOH2244 |
| A | HOH2245 |
| A | HOH2246 |
| B | ASP9 |
| B | PHE36 |
| B | PRO37 |
| B | TYR39 |
| B | PHE70 |
| B | ARG74 |
| B | ARG95 |
| B | ASN100 |
| B | TYR103 |
| B | TYR165 |
| B | GLU166 |
| B | MG301 |
| B | TMP302 |
| B | ACT305 |
| B | HOH2022 |
| B | HOH2023 |
| B | HOH2026 |
| B | HOH2029 |
| B | HOH2030 |
| B | HOH2031 |
| site_id | BC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE TMP B 302 |
| Chain | Residue |
| A | ASP9 |
| A | TYR39 |
| A | PHE70 |
| A | ARG74 |
| A | ARG95 |
| A | ASN100 |
| A | TYR103 |
| A | TYR165 |
| A | MG301 |
| A | TYD302 |
| A | HOH2046 |
| A | HOH2193 |
| A | HOH2243 |
| A | HOH2244 |
| B | ASP9 |
| B | PRO37 |
| B | TYR39 |
| B | PHE70 |
| B | ARG74 |
| B | ARG95 |
| B | ASN100 |
| B | TYR103 |
| B | TYR165 |
| B | MG301 |
| B | HOH2026 |
| B | HOH2029 |
| B | HOH2030 |
| B | HOH2031 |
Functional Information from PROSITE/UniProt
| site_id | PS01331 |
| Number of Residues | 13 |
| Details | THYMIDYLATE_KINASE Thymidylate kinase signature. ILDRYvaSNaAYS |
| Chain | Residue | Details |
| A | ILE92-SER104 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Region: {"description":"LID"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
