Iron in PDB 5fw4: Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds

All present enzymatic activity of Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds:
1.11.1.19;

The structure of Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds, PDB code: 5fw4 was solved by R.Rahmanpour, D.Rea, S.Jamshidi, V.Fulop, T.D.H.Bugg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.21 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	143.360, 110.210, 46.730, 90.00, 90.00, 90.00
R / Rfree (%)	20.426 / 24.927

The binding sites of Iron atom in the Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds (pdb code 5fw4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds, PDB code: 5fw4:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:24.7 occ:1.00 FE A:HEM401 0.0 24.7 1.0 ND A:HEM401 1.9 23.5 1.0 NA A:HEM401 2.0 22.8 1.0 NC A:HEM401 2.1 24.7 1.0 NB A:HEM401 2.1 22.8 1.0 NE2 A:HIS299 2.2 24.1 1.0 O2 A:OXY402 2.4 29.3 1.0 C4D A:HEM401 2.9 23.5 1.0 C1D A:HEM401 3.0 25.2 1.0 C1A A:HEM401 3.0 22.8 1.0 C4B A:HEM401 3.0 22.4 1.0 CE1 A:HIS299 3.0 24.8 1.0 C4A A:HEM401 3.0 21.4 1.0 C4C A:HEM401 3.0 22.1 1.0 C1B A:HEM401 3.0 21.1 1.0 C1C A:HEM401 3.1 23.3 1.0 CD2 A:HIS299 3.2 25.5 1.0 CHA A:HEM401 3.4 21.9 1.0 O1 A:OXY402 3.4 36.8 1.0 CHC A:HEM401 3.4 22.2 1.0 CHD A:HEM401 3.4 23.9 1.0 CHB A:HEM401 3.5 20.2 1.0 ND1 A:HIS299 4.2 25.6 1.0 C3D A:HEM401 4.2 25.2 1.0 C2A A:HEM401 4.2 23.0 1.0 C3A A:HEM401 4.2 20.5 1.0 C2D A:HEM401 4.2 24.5 1.0 C3C A:HEM401 4.2 21.5 1.0 C2C A:HEM401 4.2 21.9 1.0 C2B A:HEM401 4.3 21.0 1.0 C3B A:HEM401 4.3 22.5 1.0 CG A:HIS299 4.3 24.7 1.0 CD A:ARG315 4.8 28.9 1.0 NE A:ARG315 4.9 30.6 1.0

Iron binding site 2 out of 2 in the Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:25.8 occ:1.00 FE B:HEM401 0.0 25.8 1.0 ND B:HEM401 1.9 27.3 1.0 NA B:HEM401 2.0 26.5 1.0 NB B:HEM401 2.1 23.4 1.0 NC B:HEM401 2.1 27.1 1.0 NE2 B:HIS299 2.2 25.8 1.0 O2 B:OXY402 2.8 46.9 1.0 C4D B:HEM401 2.9 26.9 1.0 C1D B:HEM401 2.9 28.9 1.0 C1A B:HEM401 3.0 26.8 1.0 C4B B:HEM401 3.0 22.2 1.0 C4A B:HEM401 3.0 25.7 1.0 C1B B:HEM401 3.1 23.6 1.0 CE1 B:HIS299 3.1 26.8 1.0 C1C B:HEM401 3.1 23.6 1.0 C4C B:HEM401 3.1 24.8 1.0 CD2 B:HIS299 3.2 27.0 1.0 CHA B:HEM401 3.4 27.1 1.0 CHC B:HEM401 3.4 22.6 1.0 CHB B:HEM401 3.4 22.6 1.0 CHD B:HEM401 3.5 26.9 1.0 O1 B:OXY402 3.9 44.5 1.0 C2D B:HEM401 4.2 29.2 1.0 C2A B:HEM401 4.2 27.1 1.0 C3D B:HEM401 4.2 29.7 1.0 C3A B:HEM401 4.2 26.5 1.0 ND1 B:HIS299 4.2 25.3 1.0 CG B:HIS299 4.3 26.0 1.0 C2B B:HEM401 4.3 23.1 1.0 C3B B:HEM401 4.3 21.7 1.0 C2C B:HEM401 4.3 24.5 1.0 C3C B:HEM401 4.3 24.3 1.0 NE B:ARG315 4.7 34.4 1.0 CD B:ARG315 4.8 31.2 1.0

R.Rahmanpour, D.Rea, S.Jamshidi, V.Fulop, T.D.H.Bugg. Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds. Arch.Biochem.Biophys. V. 594 54 2016.
ISSN: ISSN 0003-9861
PubMed: 26901432
DOI: 10.1016/J.ABB.2016.02.019