Iron in PDB 6vdu: Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Iron(III) Deuteroporphyrin IX and Substrate Trichlorophenol

The structure of Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Iron(III) Deuteroporphyrin IX and Substrate Trichlorophenol, PDB code: 6vdu was solved by R.A.Ghiladi, V.S.De Serrano, A.Mcguire, T.Malewschik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.65 / 1.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.174, 67.901, 67.905, 90, 90, 90
R / Rfree (%)	19.7 / 26.1

The structure of Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Iron(III) Deuteroporphyrin IX and Substrate Trichlorophenol also contains other interesting chemical elements:

Chlorine

(Cl)

6 atoms

The binding sites of Iron atom in the Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Iron(III) Deuteroporphyrin IX and Substrate Trichlorophenol (pdb code 6vdu). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Iron(III) Deuteroporphyrin IX and Substrate Trichlorophenol, PDB code: 6vdu:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Iron(III) Deuteroporphyrin IX and Substrate Trichlorophenol


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Iron(III) Deuteroporphyrin IX and Substrate Trichlorophenol within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:84.5 occ:0.60 FE A:FDE201 0.0 84.5 0.6 NA A:FDE201 2.0 80.6 0.6 NB A:FDE201 2.1 75.5 0.6 NC A:FDE201 2.1 81.3 0.6 ND A:FDE201 2.1 82.1 0.6 C1A A:FDE201 3.0 80.8 0.6 C4A A:FDE201 3.1 79.8 0.6 C1B A:FDE201 3.1 77.6 0.6 C4B A:FDE201 3.1 75.4 0.6 C4D A:FDE201 3.1 83.0 0.6 C4C A:FDE201 3.1 80.3 0.6 C1D A:FDE201 3.1 84.3 0.6 C1C A:FDE201 3.1 75.3 0.6 CL4 A:T6C202 3.4 62.2 0.9 CHA A:FDE201 3.5 82.5 0.6 CHB A:FDE201 3.5 79.5 0.6 CHD A:FDE201 3.5 81.3 0.6 CHC A:FDE201 3.5 76.9 0.6 C5 A:T6C202 4.2 64.5 0.9 C2A A:FDE201 4.3 78.6 0.6 C3A A:FDE201 4.3 77.3 0.6 CD1 A:LEU92 4.3 80.3 1.0 C4 A:T6C202 4.4 59.9 0.9 C2B A:FDE201 4.4 74.8 0.6 C3B A:FDE201 4.4 74.5 0.6 C2C A:FDE201 4.4 73.2 0.6 CG2 A:VAL59 4.4 31.0 1.0 C3C A:FDE201 4.4 71.7 0.6 C3D A:FDE201 4.5 87.1 0.6 C2D A:FDE201 4.5 87.5 0.6 CG A:LEU92 4.8 78.3 1.0 CZ A:PHE97 4.9 56.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Iron(III) Deuteroporphyrin IX and Substrate Trichlorophenol


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Iron(III) Deuteroporphyrin IX and Substrate Trichlorophenol within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:80.9 occ:0.60 FE B:FDE201 0.0 80.9 0.6 NA B:FDE201 2.0 76.4 0.6 NB B:FDE201 2.1 73.4 0.6 NC B:FDE201 2.1 75.2 0.6 ND B:FDE201 2.1 78.5 0.6 C4A B:FDE201 3.0 77.9 0.6 C1A B:FDE201 3.0 78.3 0.6 C1B B:FDE201 3.1 73.3 0.6 C4B B:FDE201 3.1 73.5 0.6 C4C B:FDE201 3.1 74.2 0.6 C4D B:FDE201 3.1 77.9 0.6 C1C B:FDE201 3.2 70.6 0.6 C1D B:FDE201 3.2 78.2 0.6 CL4 B:T6C202 3.3 58.1 0.8 CD1 B:LEU92 3.5 73.9 1.0 CHA B:FDE201 3.5 77.3 0.6 CHB B:FDE201 3.5 73.8 0.6 CHD B:FDE201 3.5 74.8 0.6 CHC B:FDE201 3.5 72.2 0.6 C2A B:FDE201 4.3 79.2 0.6 C3A B:FDE201 4.3 79.8 0.6 CG2 B:VAL59 4.3 29.5 1.0 C2B B:FDE201 4.4 73.9 0.6 C3B B:FDE201 4.4 74.0 0.6 C3C B:FDE201 4.4 67.7 0.6 C2C B:FDE201 4.4 67.2 0.6 CZ B:PHE97 4.5 55.3 1.0 C3D B:FDE201 4.5 77.6 0.6 C2D B:FDE201 4.5 79.2 0.6 C4 B:T6C202 4.5 53.9 0.8 CE1 B:PHE97 4.6 55.0 1.0 C3 B:T6C202 4.6 57.6 0.8 CG B:LEU92 4.7 76.6 1.0 CG1 B:VAL59 4.7 28.5 1.0 CD2 B:LEU92 4.9 76.3 1.0

A.H.Mcguire, A.R.Petit, J.Kang, T.Malewschik, V.De Serrano, L.M.Carey, R.A.Ghiladi. Nonnative Heme Incorporation Into Multifunctional Globin Increases Peroxygenase Activity An Order and Magnitude Compared to Native Enzyme To Be Published.