Iron in PDB 3mm1: Dye-Decolorizing Peroxidase (Dyp) D171N

All present enzymatic activity of Dye-Decolorizing Peroxidase (Dyp) D171N:
1.11.1.19;

The structure of Dye-Decolorizing Peroxidase (Dyp) D171N, PDB code: 3mm1 was solved by Y.Sugano, T.Yoshida, H.Tsuge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.85 / 1.42
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.980, 95.972, 50.309, 90.00, 103.71, 90.00
R / Rfree (%)	16.9 / 18.7

The binding sites of Iron atom in the Dye-Decolorizing Peroxidase (Dyp) D171N (pdb code 3mm1). 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 Dye-Decolorizing Peroxidase (Dyp) D171N, PDB code: 3mm1:

Iron binding site 1 out of 1 in the Dye-Decolorizing Peroxidase (Dyp) D171N


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Dye-Decolorizing Peroxidase (Dyp) D171N within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:4.0 occ:1.00 FE A:HEM501 0.0 4.0 1.0 NA A:HEM501 2.0 4.3 1.0 NC A:HEM501 2.0 3.5 1.0 ND A:HEM501 2.0 3.4 1.0 NB A:HEM501 2.0 3.5 1.0 NE2 A:HIS308 2.1 4.0 1.0 O A:HOH1201 2.2 9.0 1.0 C4A A:HEM501 3.0 4.5 1.0 C4D A:HEM501 3.1 4.2 1.0 C1A A:HEM501 3.1 3.6 1.0 C1C A:HEM501 3.1 3.7 1.0 C4C A:HEM501 3.1 4.2 1.0 CE1 A:HIS308 3.1 4.3 1.0 C4B A:HEM501 3.1 3.1 1.0 C1D A:HEM501 3.1 3.2 1.0 C1B A:HEM501 3.1 4.0 1.0 CD2 A:HIS308 3.2 4.5 1.0 CHA A:HEM501 3.4 3.8 1.0 CHC A:HEM501 3.4 3.4 1.0 CHB A:HEM501 3.4 4.4 1.0 CHD A:HEM501 3.4 4.0 1.0 ND1 A:HIS308 4.2 4.0 1.0 NH1 A:ARG329 4.2 5.0 1.0 C3A A:HEM501 4.3 4.2 1.0 C2C A:HEM501 4.3 4.1 1.0 C2A A:HEM501 4.3 4.5 1.0 C3C A:HEM501 4.3 4.4 1.0 C3D A:HEM501 4.3 4.0 1.0 CG A:HIS308 4.3 3.7 1.0 C3B A:HEM501 4.3 4.0 1.0 C2B A:HEM501 4.3 4.3 1.0 C2D A:HEM501 4.3 5.0 1.0 O A:HOH1200 4.4 8.4 1.0 CD A:ARG329 4.9 5.6 1.0 CE1 A:PHE356 5.0 6.0 1.0

T.Yoshida, H.Tsuge, H.Konno, T.Hisabori, Y.Sugano. The Catalytic Mechanism of Dye-Decolorizing Peroxidase Dyp May Require the Swinging Movement of An Aspartic Acid Residue Febs J. V. 278 2387 2011.
ISSN: ISSN 1742-464X
PubMed: 21569205
DOI: 10.1111/J.1742-4658.2011.08161.X