Crystallization (Comment) | Organism |
---|---|
molecular modeling based on Escherichia coli crystal structure, and molecular dynamics simulation. The binding pocket is composed of residues Lys13, Thr14, Ala17, Leu18, Ile21, Arg26, Lys35, Glu38, Pro39, Glu40, Asp103, Leu105, Ile133, Gly135, Gly136, Gln137 and Thr138 | Pyrococcus horikoshii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(2R,3S,4R,5R)-2-(aminomethyl)-5-(hydroxymethyl)oxolane-3,4-diol | i.e. NCI_121957. Molecular docking, compound interacts with residues Lys35, Thr14, Gly136, Glu137 and Asp103, best inhibitor identified | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O58054 | - |
- |
Pyrococcus horikoshii OT-3 | O58054 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
AIRS | - |
Pyrococcus horikoshii |
aminoimidazole ribonucleotide synthetase | - |
Pyrococcus horikoshii |
PurM | - |
Pyrococcus horikoshii |