EC Number   |
|---|
   3.4.11.18 | - |
| 3.4.11.18 | 1.8 resolution crystal structure of free enzyme and enzyme complexed with fumagillin. Crystals are grown in 1 to 2 weeks at 4°C from sitting drops, with a protein concentration of 12 mg/ml |
| 3.4.11.18 | apo-enzyme without any active-site metals |
| 3.4.11.18 | apo-form of enzyme and modeling of inhibitor 2,2'-bipyridine. One of the rings of 2,2'-bipyridine that points into the S1 pocket is surrounded by residues Tyr60, Tyr63, Trp218, and Cys68, while the other ring points towards the surface of the protein that does not make any contact with the protein, except with the metal ion |
| 3.4.11.18 | both apo- and methionine-bound forms |
| 3.4.11.18 | complexed with inhibitor, sitting drop vapour diffusion method with 15-20% tert-butyl alcohol containing 0.4-0.1 M aqueous sodium citrate at pH 5.5 |
| 3.4.11.18 | contains two molecules in the asymmetric unit and well ordered inserts with structural features that corroborate the possible posttranslational modification. Both the new inserts present structurally align with the P-X-X-P motif found in other type I Metionine aminopeptidases as well as the 60 amino acid insert in the human type II. In addition, one of the beta-hairpins within in the catalytic domain undergoes a flip placing a residue which is essential for enzyme activity away from the active site and the beta-hairpin loop of this secondary structure in the active site obstructing substrate binding |
| 3.4.11.18 | crystal structure of MetAP-1 as an apoenzyme and its complexes with various 1,2,4-triazole-based derivatives at high-resolution. Form 1 crystals are grown in the presence of 0.1 mM NiCl2 with 25% PEG 3350, 100 mM bis-Tris, pH 6.5, 200 mM LiSO4. Form 2 crystals are grown in the absence of metal ions using 25% PEG, 100 mM bis-Tris, pH 5.5, 200 mM ammonium acetate as precipitating agent |
| 3.4.11.18 | crystal structure of N-terminally truncated MetAP1 in complex with inhibitor 4-[4-(4-methoxyphenyl)piperazin-1-yl]-2-(pyridin-2-yl)quinazoline and Co(II) |
| 3.4.11.18 | electronic absorption spectrum in the absence and presence of both nitric oxide and the substrate-analog butaneboronic acid. Both bind to the catalytic Fe(II)-center of enzyme forming a complex that mimics an intermediate step between the Michaelis complex and the tetrahedral transition-state |
