116
|
306
|
1h5jA |
X-ray induced reduction of horseradish peroxidase c1a compound iii (67-78% dose) |
118
|
306
|
1h5fA |
X-ray induced reduction of horseradish peroxidase c1a compound iii (22-33% dose) |
116
|
306
|
1h5lA |
X-ray induced reduction of horseradish peroxidase c1a compound iii (89-100% dose) |
118
|
306
|
1h5dA |
X-ray induced reduction of horseradish peroxidase c1a compound iii (0-11% dose) |
119
|
306
|
1hchA |
Structure of horseradish peroxidase c1a compound i |
118
|
306
|
1h5hA |
X-ray induced reduction of horseradish peroxidase c1a compound iii (44-56% dose) |
120
|
306
|
1gwuA |
Recombinant horseradish peroxidase c1a ala140gly |
115
|
308
|
1gx2A |
Recombinant horseradish peroxidase phe209ser complex with benzhydroxamic acid |
118
|
307
|
1gwtA |
Recombinant horseradish peroxidase c1a phe221met |
113
|
306
|
1gw2A |
Recombinant horseradish peroxidase c1a thr171ser in complex with ferulic acid |
116
|
336
|
1gzbA |
Peroxidase |
113
|
307
|
1gwoA |
Recombinant horseradish peroxidase c1a ala170gln |
111
|
336
|
1gzaA |
Peroxidase |
115
|
336
|
1h3jA |
Structure of recombinant coprinus cinereus peroxidase determined to 2.0 a |
119
|
306
|
1h5iA |
X-ray induced reduction of horseradish peroxidase c1a compound iii (56-67% dose) |
116
|
306
|
1h55A |
Structure of horseradish peroxidase c1a compound ii |
118
|
306
|
1h5aA |
Structure of ferric horseradish peroxidase c1a in complex with acetate |
118
|
306
|
1h57A |
Structure of horseradish peroxidase c1a compound iii |
118
|
306
|
1h5cA |
X-ray induced reduction of horseradish peroxidase c1a compound iii (100-200% dose) |
117
|
306
|
1h58A |
Structure of ferrous horseradish peroxidase c1a |
108
|
304
|
1fhfA |
The structure of soybean peroxidase |
102
|
294
|
1jdrA |
Crystal structure of a proximal domain potassium binding variant of cytochrome c peroxidase |
109
|
293
|
1ebeA |
Laue diffraction study on the structure of cytochrome c peroxidase compound i |
109
|
291
|
1dspA |
Cytochrome c peroxidase h175g mutant, imidazole complex at ph 7, room temperature. |
109
|
292
|
1dseA |
Cytochrome c peroxidase h175g mutant, imidazole complex, with phosphate bound, ph 6, 100k |
106
|
291
|
1dsgA |
Cytochrome c peroxidase h175g mutant, imidazole complex at ph 5, room temperature. |
109
|
294
|
1jciA |
Stabilization of the engineered cation-binding loop in cytochrome c peroxidase (ccp) |
108
|
291
|
1dsoA |
Cytochrome c peroxidase h175g mutant, imidazole complex at ph 6, room temperature. |
111
|
292
|
1ds4A |
Cytochrome c peroxidase h175g mutant, imidazole complex, ph 6, 100k |
108
|
291
|
1dccA |
2.2 angstrom structure of oxyperoxidase: a model for the enzyme:peroxide complex |
111
|
291
|
1dj5A |
Crystal structure of r48a mutant of cytochrome c peroxidase with n-hydroxyguanidine bound |
110
|
291
|
1dj1A |
Crystal structure of r48a mutant of cytochrome c peroxidase |
118
|
336
|
1ck6A |
Binding mode of salicylhydroxamic acid to arthromyces ramosus peroxidase |
105
|
291
|
1cpeA |
A cation binding motif stabilizes the compound i radical of cytochrome c peroxidase |
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 |
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 |
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 |