EC Number   |
Reference |
|---|
    2.4.2.18 | - |
638676 |
| 2.4.2.18 | crystal structures of the wild-type enzyme complexed to its two natural substrates anthranilate and 5-phosphoribosyl-1-pyrophosphate/Mg2+ |
680670 |
| 2.4.2.18 | free enzyme and in the presence of Zn2+, hanging drop vapor diffusion method, using 0.2 M sodium acetate (pH 7.5), 20% (w/v) PEG 3350 |
759199 |
| 2.4.2.18 | hanging drop vapor diffusion method |
638678 |
| 2.4.2.18 | hanging drop vapor diffusion method, complexed with Mn2+ diphosphate |
638679 |
| 2.4.2.18 | hanging-drop method, crystals of ssTrpD diffract to better than 2.6 A resolution |
638678 |
| 2.4.2.18 | in complex with inhibitors, hanging drop vapor diffusion method, using 0.2 M imidazole. malate, pH 7.0, 15% (w/v) PEG 4000 |
759106 |
| 2.4.2.18 | mutant D83G/F149S in complex with 5-phospho-alpha-D-ribose 1-diphosphate and Mn2+, to 2.25 A resolution. Protein backbone of mutant D83G/F149S shows no detectable differences to the wild-type enzyme, whereas 5-phospho-alpha-D-ribose 1-diphosphate bound to mutant D83G/F149S adopts an extended conformation that contrasts markedly with the S compact shape observed in complexes of the wild-type enzyme |
702308 |
| 2.4.2.18 | mutant enzymes N138A, P180A, R193L, R193A, R194A, and G107P, hanging drop vapor diffusion method, using |
735688 |
| 2.4.2.18 | mutant M47D, structurally very similar to wild-type (rms deviation of 0.7 A for most of equivalent C(alpha) atoms) but reduced buried surface area per subunit compared to wild-type homodimer, Aps47 protonated at pH 6, crystals of space group P2 with four molecules (two homodimers) per asymmetric unit and A2 pseudo-symmetry, unit cell parameters a=91.6 A, b=65.9 A, c=115.7 A, beta=107.4°, 45% (v/v) solvent content, hanging drop method: 1 microlitre protein solution (5 mg/ml) + 1 microlitre reservior solution (50 mM MES pH 6.0, 18% (v/v) PEG, 5% (v/v) glycerol), room temperature, 72 h |
693629 |
