101
|
291
|
1ccgA |
Construction of a bis-aquo heme enzyme and replacement with exogenous ligand |
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 |
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 |
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 |
91
|
249
|
1apxA |
Crystal structure of recombinant ascorbate peroxidase |
99
|
291
|
1aeqA |
Variation in the strength of a ch to o hydrogen bond in an artificial protein cavity (2-ethylimidazole) |
99
|
291
|
1aefA |
Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (3-aminopyridine) |
101
|
291
|
1a2fA |
Probing the strength and character of an asp-his-x hydrogen bond by introducing buried charges |
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) |
37
|
105
|
1abvA |
N-terminal domain of the delta subunit of the f1f0-atp synthase from escherichia coli, nmr, minimized average structure |
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
|
1a2gA |
Probing the strength and character of an asp-his-x hydrogen bond by introducing buried charges |
99
|
291
|
1aehA |
Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (2-amino-4-methylthiazole) |
99
|
291
|
1aevA |
Introduction of novel substrate oxidation into cytochrome c peroxidase by cavity complementation: oxidation of 2-aminothiazole and covalent modification of the enzyme (2-aminothiazole) |
99
|
291
|
1aebA |
Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (3-methylthiazole) |
95
|
291
|
1aa4A |
Specificity of ligand binding in a buried polar cavity of cytochrome c peroxidase |
99
|
291
|
1aekA |
Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (indoline) |
96
|
291
|
1aeoA |
Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (2-aminopyridine) |
96
|
291
|
1aeuA |
Specificity of ligand binding in a polar cavity of cytochrome c peroxidase (2-methylimidazole) |
99
|
291
|
1ac8A |
Variation in the strength of a ch to o hydrogen bond in an artificial protein cavity (3,4,5-trimethylthiazole) |
96
|
291
|
1aenA |
Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (2-amino-5-methylthiazole) |
99
|
291
|
1aedA |
Specificity of ligand binding to a buried polar cavity at the active site of cytochrome c peroxidase (3,4-dimethylthiazole) |