EC Number   |
|---|
   3.4.17.21 | GCPIII ectodomain in a pseudo-unliganded state and in a complex with product L-glutamate, or the phosphapeptide transition state mimetic (2S,3'S)-[[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl]-pentanedioic acid, or quisqualic acid, a glutamate biostere, X-ray diffraction structure determination and analysis at 1.29-1.56 A resolution, modelling |
| 3.4.17.21 | hanging-drop vapor-diffusion method, crystal structures of human glutamate carboxypeptidase II in complex with a series of phosphoramidate-based inhibitors harboring effector functions of diverse physicochemical characteristics |
| 3.4.17.21 | in complex with inhibitors N-2-([(1S)-1-carboxy-2-(furan-2-yl)ethyl]carbamoyl)-N-6-(4-iodobenzoyl)-L-lysine, N-2-([(1S)-1-carboxybut-3-yn-1-yl]carbamoyl)-N-6-(4-iodobenzoyl)-L-lysine, and N-([(1S)-1-carboxy-5-([(4-iodophenyl)carbonyl]amino)pentyl]carbamoyl)-L-glutamic acid, PDB entries 4OC2, 4OC3, and 3D7H, respectively |
| 3.4.17.21 | prostate-specific membrane antigen crystal structure analysis |
| 3.4.17.21 | purified recombinant extracellular portion of the enzyme, comprising residues 44-750, in complex with GPI-18431, a iodobenzyl derivative of inhibitor 2-PMPA, hanging drop vapour diffusion method, room temperature, 0.002 ml protein solution, containing 0.2 mM GPI-18431, is mixed with 0.002 ml well solution containing 20 mM HEPES, pH 7.5, 0.2 M NaCl, 5% w/v PEG 400, and 15%w/v PEG 1500, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.2 A resolution |
| 3.4.17.21 | purified recombinant His6-tagged extracellular portion, which contains bound Zn2+, hanging drop vapour diffusion method, 0.0008 ml of 10 mg/ml protein in 20 mM Tris, pH 7.5, is mixed with an equal volume of reservoir solution containing 18% PEG 3350, 0.2 M sodium thiocyanate, 4°C, cryoprotection by 20% glycerol, X-ray diffrcation structure determination and analysis at 3.5 A resolution |
| 3.4.17.21 | the crystal structure of GCPII(E424A) in complex with N-acetyl-L-aspartyl-L-glutamate is determined at 1.70 A resolution |
| 3.4.17.21 | the structures of human GCPII in complex with (S)-2-(3-((R)-1-carboxy-(2-methylthio)ethyl)ureido)pentanedioic acid, (S)-2-(3-((S)-1-carboxy-2-(4-hydroxy-3-iodophenyl)ethyl)ureido)pentanedioic acid, (S)-2-(3-((R)-1-carboxy-2-(4-fluorobenzylthio)ethyl)ureido)pentanedioic acid and (S)-2-(3-((S)-1-carboxy-(4-iodobenzamido)pentyl)ureido)pentanedioic acid are solved to a resolution of 1.75, 1.54, 1.69 and 1.55 A, respectively |
| 3.4.17.21 | X-ray crystal structure of glutamate carboxypeptidase II in complex with (S)-2-(3-((S)-1-carboxy-5-(1,2-dicarba-closo-dodecarboranylamido) pentyl)ureido)pentanedioic acid at 1.79 A resolution. The X-ray analysis reveals that the bulky closo-carborane cluster is located in the spacious entrance funnel region of the enzyme, indicating that the carborane cluster can be further structurally modified to identify promising lead structures of novel glutamate carboxypeptidase II inhibitors |
| 3.4.17.21 | X-ray structure of human glutamate carboxypeptidase II in complex with hydroxamate-based inhibitors |
