1N5K
CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS THYMIDYLATE KINASE CRYSTALLIZED IN SODIUM MALONATE (RESOLUTION 2.1 A)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004798 | molecular_function | thymidylate 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 | 0016310 | biological_process | phosphorylation |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046044 | biological_process | TMP metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004798 | molecular_function | thymidylate 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 | 0016310 | biological_process | phosphorylation |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046044 | biological_process | TMP metabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 410 |
Chain | Residue |
A | GLY10 |
A | ALA11 |
A | GLY12 |
A | LYS13 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 412 |
Chain | Residue |
B | GLY10 |
B | ALA11 |
B | GLY12 |
B | LYS13 |
B | ARG14 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 414 |
Chain | Residue |
A | ARG122 |
A | ILE123 |
A | ARG127 |
B | ASN111 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 413 |
Chain | Residue |
B | ASP9 |
B | TMP411 |
B | HOH471 |
B | HOH513 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TMP A 409 |
Chain | Residue |
A | ASP9 |
A | PRO37 |
A | TYR39 |
A | PHE70 |
A | ARG74 |
A | ARG95 |
A | ASN100 |
A | TYR103 |
A | TYR165 |
A | HOH435 |
A | HOH498 |
A | HOH516 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE TMP B 411 |
Chain | Residue |
B | ASP9 |
B | PHE36 |
B | PRO37 |
B | TYR39 |
B | LEU52 |
B | PHE70 |
B | ARG74 |
B | ARG95 |
B | ASN100 |
B | TYR103 |
B | TYR165 |
B | MG413 |
B | HOH414 |
B | HOH470 |
B | HOH474 |
B | HOH512 |
B | HOH513 |
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 | 22 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY7 | |
A | TYR165 | |
A | GLU166 | |
B | GLY7 | |
B | ASP9 | |
B | TYR39 | |
B | PHE70 | |
B | ARG74 | |
B | ARG95 | |
B | ASN100 | |
B | TYR103 | |
A | ASP9 | |
B | ASP163 | |
B | TYR165 | |
B | GLU166 | |
A | TYR39 | |
A | PHE70 | |
A | ARG74 | |
A | ARG95 | |
A | ASN100 | |
A | TYR103 | |
A | ASP163 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000255 |
Chain | Residue | Details |
A | ARG153 | |
B | ARG153 |