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Iron in PDB 1h7k: Formation of A Tyrosyl Radical Intermediate in Proteus Mirabilis Catalase By Directed Mutagenesis and Consequences For Nucleotide Reactivity

Enzymatic 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: 1h7k was solved by P.Andreoletti, S.Gambarelli, J.Gaillard, G.Sainz, V.Stojanoff, H.M.Jouve, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.26 / 2.40
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 110.000, 110.000, 251.200, 90.00, 90.00, 120.00
R / Rfree (%) 23.7 / 24

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 1h7k). 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: 1h7k:

Iron binding site 1 out of 1 in 1h7k

Go back to Iron Binding Sites List in 1h7k
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

A full contact list of Iron with other atoms in the Fe binding site number 1 of Formation of A Tyrosyl Radical Intermediate in Proteus Mirabilis Catalase By Directed Mutagenesis and Consequences For Nucleotide Reactivity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:27.0
occ:1.00
 FE A:HEM600 0.0 27.0 1.0
ND A:HEM600 2.0 22.5 1.0
NB A:HEM600 2.0 24.7 1.0
NC A:HEM600 2.0 22.4 1.0
NA A:HEM600 2.0 24.2 1.0
OH A:TYR337 2.1 21.4 1.0
C1D A:HEM600 3.0 24.0 1.0
C4D A:HEM600 3.0 24.2 1.0
C1C A:HEM600 3.0 24.7 1.0
C1B A:HEM600 3.0 24.5 1.0
C4B A:HEM600 3.0 25.1 1.0
C1A A:HEM600 3.0 24.3 1.0
C4A A:HEM600 3.1 24.0 1.0
C4C A:HEM600 3.1 23.7 1.0
CZ A:TYR337 3.1 22.7 1.0
CHD A:HEM600 3.4 21.9 1.0
CHB A:HEM600 3.4 24.9 1.0
CHC A:HEM600 3.4 25.1 1.0
CHA A:HEM600 3.4 23.9 1.0
CE2 A:TYR337 3.8 24.9 1.0
CE1 A:TYR337 4.0 23.1 1.0
NE A:ARG333 4.1 30.6 1.0
NH2 A:ARG333 4.1 30.8 1.0
C3B A:HEM600 4.2 24.5 1.0
C2D A:HEM600 4.2 23.1 1.0
C2B A:HEM600 4.3 24.1 1.0
C2C A:HEM600 4.3 22.6 1.0
C3D A:HEM600 4.3 23.5 1.0
C3C A:HEM600 4.3 21.8 1.0
C2A A:HEM600 4.3 24.3 1.0
C3A A:HEM600 4.3 24.0 1.0
O A:HOH2024 4.5 65.9 1.0
CZ A:ARG333 4.6 30.1 1.0
CZ A:PHE140 4.6 38.0 1.0
CD2 A:HIS54 4.8 22.3 1.0
NE2 A:HIS54 4.9 21.3 1.0

Reference:

P.Andreoletti, S.Gambarelli, G.Sainz, V.Stojanoff, C.White, G.Desfonds, J.Gagnon, J.Gaillard, H.M.Jouve. Formation of A Tyrosyl Radical Intermediate in Proteus Mirabilis Catalase By Directed Mutagenesis and Consequences For Nucleotide Reactivity. Biochemistry V. 40 13734 2001.
ISSN: ISSN 0006-2960
PubMed: 11695923
DOI: 10.1021/BI010687F
Page generated: Sat Aug 3 07:18:18 2024

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