EC Number   |
Reference |
|---|
    6.3.5.13 | crystal structure of the GatD/MurT complex reveals an open, boomerang-shaped conformation in which GatD is docked onto one end of MurT. Putative active site residues cluster at the interface between GatD and MurT and are contributed by both proteins |
752234 |
| 6.3.5.13 | native and the selenomethionine-derivative proteins, crystals diffract beyond 1.85 and 2.25 A , respectively, and belong to space group P212121 |
749506 |
| 6.3.5.13 | structure of subunit GatD, at 1.85 A resolution. A glutamine molecule is found close to the active site funnel, hydrogen-bonded to the conserved residue R128 |
752244 |
| 6.3.5.13 | structure of the MurT/GatD complex at 3.0 A resolution. MurT has central and C-terminal domains similar to Mur ligases with a cysteine-rich insertion, which probably binds zinc, contributing to the interface with GatD. GatD is a glutaminase providing ammonia that is likely channeled to the MurT active site through a cavity network |
751671 |
