Manganese in PDB 6vdx: Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Manganese(III)- Porphyrin and Substrate Trichlorophenol

The structure of Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Manganese(III)- Porphyrin and Substrate Trichlorophenol, PDB code: 6vdx 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)	44.64 / 1.53
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.365, 67.585, 67.626, 90, 90, 90
R / Rfree (%)	16.5 / 23.7

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

Chlorine

(Cl)

6 atoms

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

Manganese binding site 1 out of 2 in the Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Manganese(III)- Porphyrin and Substrate Trichlorophenol


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Manganese(III)- Porphyrin and Substrate Trichlorophenol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn305 b:22.5 occ:1.00 MN A:MNR305 0.0 22.5 1.0 NA A:MNR305 2.0 20.5 1.0 ND A:MNR305 2.0 23.2 1.0 NB A:MNR305 2.1 20.3 1.0 NC A:MNR305 2.1 21.5 1.0 NE2 A:HIS89 2.3 23.4 1.0 C4D A:MNR305 3.0 25.0 1.0 C1A A:MNR305 3.1 22.4 1.0 C1D A:MNR305 3.1 24.9 1.0 C4A A:MNR305 3.1 19.9 1.0 C4C A:MNR305 3.1 26.2 1.0 C4B A:MNR305 3.1 22.4 1.0 C1C A:MNR305 3.1 20.3 1.0 C1B A:MNR305 3.2 22.7 1.0 CD2 A:HIS89 3.2 25.3 1.0 CE1 A:HIS89 3.3 28.4 1.0 CHA A:MNR305 3.4 20.1 1.0 CL4 A:T6C301 3.4 42.1 0.8 CHD A:MNR305 3.5 23.3 1.0 CHC A:MNR305 3.5 23.2 1.0 CHB A:MNR305 3.5 19.8 1.0 C3D A:MNR305 4.3 23.9 1.0 C3C A:MNR305 4.4 23.0 1.0 CG2 A:VAL59 4.4 16.4 1.0 C2D A:MNR305 4.4 25.8 1.0 C3A A:MNR305 4.4 21.2 1.0 C2A A:MNR305 4.4 23.5 1.0 CG A:HIS89 4.4 28.4 1.0 ND1 A:HIS89 4.4 27.1 1.0 C3B A:MNR305 4.4 22.8 1.0 C2C A:MNR305 4.4 19.5 1.0 C2B A:MNR305 4.5 22.7 1.0 C4 A:T6C301 4.5 39.2 0.8 C5 A:T6C301 4.6 37.2 0.8 CE A:MET86 4.8 24.9 1.0 CG1 A:VAL59 4.9 16.3 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Manganese(III)- Porphyrin and Substrate Trichlorophenol


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Dehaloperoxidase B in Complex with Cofactor Manganese(III)- Porphyrin and Substrate Trichlorophenol within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn304 b:16.2 occ:1.00 MN B:MNR304 0.0 16.2 1.0 NB B:MNR304 2.0 13.4 1.0 NA B:MNR304 2.0 13.8 1.0 ND B:MNR304 2.1 14.9 1.0 NC B:MNR304 2.1 16.5 1.0 NE2 B:HIS89 2.2 16.9 1.0 C4A B:MNR304 3.1 16.1 1.0 C4D B:MNR304 3.1 14.7 1.0 C4C B:MNR304 3.1 16.0 1.0 C1D B:MNR304 3.1 12.8 1.0 C4B B:MNR304 3.1 14.2 1.0 C1B B:MNR304 3.1 14.7 1.0 C1A B:MNR304 3.1 15.4 1.0 C1C B:MNR304 3.1 14.3 1.0 CD2 B:HIS89 3.2 20.4 1.0 CE1 B:HIS89 3.2 18.8 1.0 CHD B:MNR304 3.5 16.9 1.0 CHC B:MNR304 3.5 15.2 1.0 CHB B:MNR304 3.5 16.2 1.0 CL4 B:T6C301 3.5 43.4 0.8 CHA B:MNR304 3.5 14.5 1.0 C3D B:MNR304 4.3 16.7 1.0 ND1 B:HIS89 4.3 15.6 1.0 C3B B:MNR304 4.3 14.7 1.0 C2A B:MNR304 4.3 15.9 1.0 C2D B:MNR304 4.3 16.1 1.0 C3A B:MNR304 4.4 15.5 1.0 C2B B:MNR304 4.4 13.2 1.0 C3C B:MNR304 4.4 18.1 1.0 CG B:HIS89 4.4 18.5 1.0 CG2 B:VAL59 4.4 13.8 1.0 C2C B:MNR304 4.5 17.0 1.0 CE B:MET86 4.8 19.3 1.0 C4 B:T6C301 4.8 26.8 0.8 C3 B:T6C301 4.8 35.0 0.8 CG1 B:VAL59 4.9 13.8 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.