EC Number   |
|---|
    6.3.2.8 | - |
| 6.3.2.8 | construction of 3-D structure using templates PDB codes 1GQQ and 1P31. Residues G125, K126, R331, and R332 within the binding pocket are important in ligand and substrate binding affinity and selectivity |
| 6.3.2.8 | crystal structure of active fully assembled substrate- and product-bound complexes. Selenomethionine-substituted enzyme preparations used for structure determination. Crystals obtained by drop vapor diffusion experiments |
| 6.3.2.8 | crystal structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase determined to 2.6 A resolution. The structure is solved by multiwavelength anomalous diffraction methods from a single selenomethionine-substituted crystal and refined to a crystallographic R factor of 0.212. Crystals of both native and SeMet-substituted EcMurC belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 73.9 A, b = 93.6 A, c = 176.8 A. The SeMet crystals give the best quality diffraction data |
| 6.3.2.8 | crystals obtained in both native and selenemethionine forms |
