Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1H-pyrrolo(2,3-b)quinoxaline | - |
Mycobacterium tuberculosis | |
9H-pyrrolo[2,3f]quinoxaline | - |
Mycobacterium tuberculosis | |
but-3-enyl diphosphate | - |
Mycobacterium tuberculosis | |
D-erythritol 1-phosphate | - |
Mycobacterium tuberculosis | |
fosmidomycin | - |
Mycobacterium tuberculosis | |
ketoclomazone | - |
Mycobacterium tuberculosis | |
methyl hydroxytriazaindolizine | - |
Mycobacterium tuberculosis | |
additional information | inhibitor screening and enzyme-inhibitor molecular docking study using enzyme structure with bound CTP and Mg2+ (PDB ID 3Q7U). The attached CTP and Mg2+ ion are deleted from the structure, followed by refinement of the protein subunit. The crucial active site residues Gly16, Arg83, Thr84, and Thy190 play a vital role in the protein-ligand stabilization process | Mycobacterium tuberculosis | |
prop-2-yn-1-yl trihydrogen diphosphate | schembl1651692 | Mycobacterium tuberculosis | |
propyl trihydrogen diphosphate | - |
Mycobacterium tuberculosis | |
pyrrolo[1,2-a]quinoxaline | - |
Mycobacterium tuberculosis | |
rosuvastatin | RST, significantly interacts at the active site of the enzyme. Active-site residues Gly16, Arg83, Thr84, and Thy190 are potentially contributing to the protein-ligand interaction | Mycobacterium tuberculosis | |
sulfanilamide | - |
Mycobacterium tuberculosis | |
triazolopyrimidine derivative | PubChem CID 330031 | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
CTP + 2-C-methyl-D-erythritol 4-phosphate | Mycobacterium tuberculosis | - |
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol | - |
? | |
CTP + 2-C-methyl-D-erythritol 4-phosphate | Mycobacterium tuberculosis H37Rv | - |
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol | - |
? | |
CTP + 2-C-methyl-D-erythritol 4-phosphate | Mycobacterium tuberculosis ATCC 25618 | - |
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WKG9 | - |
- |
Mycobacterium tuberculosis ATCC 25618 | P9WKG9 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WKG9 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
CTP + 2-C-methyl-D-erythritol 4-phosphate | - |
Mycobacterium tuberculosis | diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol | - |
? | |
CTP + 2-C-methyl-D-erythritol 4-phosphate | - |
Mycobacterium tuberculosis H37Rv | diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol | - |
? | |
CTP + 2-C-methyl-D-erythritol 4-phosphate | - |
Mycobacterium tuberculosis ATCC 25618 | diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | the beta-domains of the monomers are mainly responsible for the formation of the dimer | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
IspD | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
additional information | the enzyme's catalytic pocket, which actively participates in interaction with ligands, mainly consists of polar amino acid residues, three-dimensional modeling of the IspD protein | Mycobacterium tuberculosis |