|
85
|
322
|
1rz6A |
Di-haem cytochrome c peroxidase, form in |
|
91
|
326
|
1rz5A |
Di-haem cytochrome c peroxidase, form out |
|
109
|
294
|
1sdqA |
Structure of reduced-no adduct of mesopone cytochrome c peroxidase |
|
106
|
291
|
1rycA |
Cytochrome c peroxidase w191g from saccharomyces cerevisiae |
|
110
|
294
|
1s73A |
Crystal structure of mesopone cytochrome c peroxidase (r-isomer) [mpccp-r] |
|
109
|
294
|
1sbmA |
Crystal structure of reduced mesopone cytochrome c peroxidase (r-isomer) |
|
86
|
326
|
1nmlA |
Di-haemic cytochrome c peroxidase from pseudomonas nautica 617, form in (ph 4.0) |
|
108
|
294
|
1ml2A |
Crystal structure of a mutant variant of cytochrome c peroxidase with zn(ii)-(20-oxo-protoporphyrin ix) |
|
107
|
294
|
1mkrA |
Crystal structure of a mutant variant of cytochrome c peroxidase (plate like crystals) |
|
111
|
294
|
1mkqA |
Crystal structure of the mutant variant of cytochrome c peroxidase in the 'open' uncross-linked form |
|
112
|
294
|
1mk8A |
Crystal structure of a mutant cytochrome c peroxidase showing a novel trp-tyr covalent cross-link |
|
108
|
289
|
1kxnA |
Crystal structure of cytochrome c peroxidase with a proposed electron transfer pathway excised to form a ligand binding channel. |
|
109
|
290
|
1kxmA |
Crystal structure of cytochrome c peroxidase with a proposed electron transfer pathway excised to form a ligand binding channel. |
|
110
|
294
|
1krjA |
Engineering calcium-binding site into cytochrome c peroxidase (ccp) |
|
113
|
294
|
1kokA |
Crystal structure of mesopone cytochrome c peroxidase (mpccp) |
|
109
|
293
|
1ebeA |
Laue diffraction study on the structure of cytochrome c peroxidase compound i |
|
102
|
294
|
1jdrA |
Crystal structure of a proximal domain potassium binding variant of cytochrome c peroxidase |
|
93
|
323
|
1eb7A |
Crystal structure of the di-haem cytochrome c peroxidase from pseudomonas aeruginosa |
|
109
|
294
|
1jciA |
Stabilization of the engineered cation-binding loop in cytochrome c peroxidase (ccp) |
|
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. |
|
111
|
292
|
1ds4A |
Cytochrome c peroxidase h175g mutant, imidazole complex, ph 6, 100k |
|
108
|
291
|
1dsoA |
Cytochrome c peroxidase h175g mutant, imidazole complex at ph 6, room temperature. |
|
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 |
|
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 |
|
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 |
|
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 |
|
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 |
|
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 |
|
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 |
|
96
|
308
|
1iqcA |
Crystal structure of di-heme peroxidase from nitrosomonas europaea |
|
107
|
291
|
1bj9A |
Effect of unnatural heme substitution on kinetics of electron transfer in cytochrome c peroxidase |
|
109
|
291
|
1bejA |
Interaction between proximal and distals regions of cytochrome c peroxidase |
