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Atomistry » Iron » PDB 1h5g-1hdb » 1h6n » |
Iron in PDB 1h6n: Formation of A Tyrosyl Radical Intermediate in Proteus Mirabilis Catalase By Directed Mutagenesis and Consequences For Nucleotide ReactivityEnzymatic activity of Formation of A Tyrosyl Radical Intermediate in Proteus Mirabilis Catalase By Directed Mutagenesis and Consequences For Nucleotide Reactivity
All present enzymatic activity of Formation of A Tyrosyl Radical Intermediate in Proteus Mirabilis Catalase By Directed Mutagenesis and Consequences For Nucleotide Reactivity:
1.11.1.6; Protein crystallography data
The structure of Formation of A Tyrosyl Radical Intermediate in Proteus Mirabilis Catalase By Directed Mutagenesis and Consequences For Nucleotide Reactivity, PDB code: 1h6n
was solved by
P.Andreoletti,
G.Sainz,
M.Jaquinod,
J.Gagnon,
H.M.Jouve,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Iron Binding Sites:
The binding sites of Iron atom in the Formation of A Tyrosyl Radical Intermediate in Proteus Mirabilis Catalase By Directed Mutagenesis and Consequences For Nucleotide Reactivity
(pdb code 1h6n). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Formation of A Tyrosyl Radical Intermediate in Proteus Mirabilis Catalase By Directed Mutagenesis and Consequences For Nucleotide Reactivity, PDB code: 1h6n: Iron binding site 1 out of 1 in 1h6nGo back to Iron Binding Sites List in 1h6n
Iron binding site 1 out
of 1 in the Formation of A Tyrosyl Radical Intermediate in Proteus Mirabilis Catalase By Directed Mutagenesis and Consequences For Nucleotide Reactivity
Mono view Stereo pair view
Reference:
P.Andreoletti,
G.Sainz,
M.Jaquinod,
J.Gagnon,
H.M.Jouve.
High Resolution Structure and Biochemical Properties of A Recombinant Proteus Mirabilis Catalase Depleted in Iron. Proteins: Struct.,Funct., V. 50 261 2003GENET..
Page generated: Sun Dec 13 14:17:03 2020
ISSN: ISSN 0887-3585 PubMed: 12486720 DOI: 10.1002/PROT.10283 |
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