Found 462 chains in Genus chains table. Displaying 401 - 450. Applied filters: Proteins

Search results query: peroxidase

Total Genus Sequence Length pdb Title
107 291 1cmuA The role of aspartate-235 in the binding of cations to an artificial cavity at the radical site of cytochrome c peroxidase
107 291 1cpdA A cation binding motif stabilizes the compound i radical of cytochrome c peroxidase
107 291 1cpfA A cation binding motif stabilizes the compound i radical of cytochrome c peroxidase
107 291 1cmtA The role of aspartate-235 in the binding of cations to an artificial cavity at the radical site of cytochrome c peroxidase
106 296 1cyfA Identifying the physiological electron transfer site of cytochrome c peroxidase by structure-based engineering
100 291 1cmpA Small molecule binding to an artificially created cavity at the active site of cytochrome c peroxidase
103 291 1cpgA A cation binding motif stabilizes the compound i radical of cytochrome c peroxidase
101 291 1cmqA Small molecule binding to an artificially created cavity at the active site of cytochrome c peroxidase
97 291 1cckA Altering substrate specificity of cytochrome c peroxidase towards a small molecular substrate peroxidase by substituting tyrosine for phe 202
99 291 1ccjA Conformer selection by ligand binding observed with protein crystallography
104 291 1ccbA The asp-his-fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free-radical to the heme
103 291 1cclA Probing the strength and character of an asp-his-x hydrogen bond by introducing buried charges
116 336 1c8iA Binding mode of hydroxylamine to arthromyces ramosus peroxidase
102 291 1ccaA The asp-his-fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free-radical to the heme
98 291 1cccA The asp-his-fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free-radical to the heme
101 291 1ccgA Construction of a bis-aquo heme enzyme and replacement with exogenous ligand
104 275 1iynA Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights for its instability
98 291 1cciA How flexible are proteins? trapping of a flexible loop
103 291 1cceA Construction of a bis-aquo heme enzyme and replacement with exogenous ligand
252 714 1itkA Crystal structure of catalase-peroxidase from haloarcula marismortui
110 291 1bvaA Manganese binding mutant in cytochrome c peroxidase
112 293 1ccpA X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis
107 291 1bj9A Effect of unnatural heme substitution on kinetics of electron transfer in cytochrome c peroxidase
113 349 1b82A Pristine recomb. lignin peroxidase h8
110 348 1b85A Lignin peroxidase
119 336 1arvA Crystal structures of cyanide-and triiodide-bound forms of arthromyces ramosus peroxidase at different ph values. perturbations of active site residues and their implication in enzyme catalysis
117 309 1bgpA Crystal structure of barley grain peroxidase 1
109 291 1bejA Interaction between proximal and distals regions of cytochrome c peroxidase
102 306 1atjA Recombinant horseradish peroxidase c1a
114 336 1aruA Crystal structures of cyanide-and triiodide-bound forms of arthromyces ramosus peroxidase at different ph values. perturbations of active site residues and their implication in enzyme catalysis
118 336 1arwA Crystal structures of cyanide-and triiodide-bound forms of arthromyces ramosus peroxidase at different ph values. perturbations of active site residues and their implication in enzyme catalysis
112 336 1arpA Crystal structure of the fungal peroxidase from arthromyces ramosus at 1.9 angstroms resolution: structural comparisons with the lignin and cytochrome c peroxidases
116 336 1aryA Crystal structures of cyanide-and triiodide-bound forms of arthromyces ramosus peroxidase at different ph values. perturbations of active site residues and their implication in enzyme catalysis
110 291 1bekA Effect of unnatural heme substitution on kinetics of electron transfer in cytochrome c peroxidase
117 336 1arxA Crystal structures of cyanide-and triiodide-bound forms of arthromyces ramosus peroxidase at different ph values. perturbations of active site residues and their implication in enzyme catalysis
108 291 1beqA Interaction between proximal and distals regions of cytochrome c peroxidase
107 291 1besA Interaction between proximal and distals regions of cytochrome c peroxidase
111 349 1b80A Rec. lignin peroxidase h8 oxidatively processed
109 291 1bepA Effect of unnatural heme substitution on kinetics of electron transfer in cytochrome c peroxidase
107 291 1bemA Interaction between proximal and distals regions of cytochrome c peroxidase
91 249 1apxA Crystal structure of recombinant ascorbate peroxidase
99 291 1aemA Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (imidazo[1,2-a]pyridine)
97 291 1aetA Variation in the strength of a ch to o hydrogen bond in an artificial protein cavity (1-methylimidazole)
100 291 1aeeA Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (aniline)
95 291 1aa4A Specificity of ligand binding in a buried polar cavity of cytochrome c peroxidase
99 291 1aejA Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (1-vinylimidazole)
99 291 1aegA Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (4-aminopyridine)
99 291 1aesA Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (imidazole)
96 291 1ac4A Variation in the strength of a ch to o hydrogen bond in an artificial protein cavity (2,3,4-trimethyl-1,3-thiazole)
99 291 1aehA Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (2-amino-4-methylthiazole)