Iron in PDB 9fy7: Dye Type Peroxidase Aa From Streptomyces Lividans with N3 Ligand By Serial Electron Diffraction (Serialed)

The binding sites of Iron atom in the Dye Type Peroxidase Aa From Streptomyces Lividans with N3 Ligand By Serial Electron Diffraction (Serialed) (pdb code 9fy7). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Dye Type Peroxidase Aa From Streptomyces Lividans with N3 Ligand By Serial Electron Diffraction (Serialed), PDB code: 9fy7:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Dye Type Peroxidase Aa From Streptomyces Lividans with N3 Ligand By Serial Electron Diffraction (Serialed)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Dye Type Peroxidase Aa From Streptomyces Lividans with N3 Ligand By Serial Electron Diffraction (Serialed) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:5.4 occ:1.00 FE A:HEM502 0.0 5.4 1.0 NA A:HEM502 2.0 6.5 1.0 NB A:HEM502 2.0 5.4 1.0 ND A:HEM502 2.0 5.8 1.0 NC A:HEM502 2.1 5.5 1.0 NE2 A:HIS326 2.1 5.2 1.0 N3 A:AZI501 2.3 9.0 1.0 CE1 A:HIS326 3.0 7.9 1.0 C4A A:HEM502 3.0 6.1 1.0 C1B A:HEM502 3.0 6.6 1.0 C1A A:HEM502 3.0 7.4 1.0 C4D A:HEM502 3.0 6.6 1.0 C4B A:HEM502 3.1 5.7 1.0 C1D A:HEM502 3.1 5.9 1.0 C4C A:HEM502 3.1 6.8 1.0 C1C A:HEM502 3.1 6.2 1.0 CD2 A:HIS326 3.1 6.2 1.0 HE1 A:HIS326 3.1 9.5 1.0 N2 A:AZI501 3.2 12.5 1.0 HD2 A:HIS326 3.3 7.5 1.0 CHB A:HEM502 3.4 5.0 1.0 CHA A:HEM502 3.4 5.5 1.0 CHC A:HEM502 3.4 6.2 1.0 CHD A:HEM502 3.4 5.0 1.0 HH11 A:ARG342 3.7 8.0 1.0 NH1 A:ARG342 4.1 6.6 1.0 ND1 A:HIS326 4.1 7.8 1.0 N1 A:AZI501 4.2 10.8 1.0 HE1 A:PHE363 4.2 13.5 1.0 CG A:HIS326 4.2 6.4 1.0 C2B A:HEM502 4.2 5.5 1.0 C2A A:HEM502 4.2 4.8 1.0 C3B A:HEM502 4.2 6.7 1.0 HH12 A:ARG342 4.3 8.0 1.0 C3D A:HEM502 4.3 6.1 1.0 C3A A:HEM502 4.3 7.4 1.0 C2D A:HEM502 4.3 5.6 1.0 C2C A:HEM502 4.3 7.1 1.0 HHB A:HEM502 4.3 6.0 1.0 C3C A:HEM502 4.3 6.5 1.0 HHA A:HEM502 4.3 6.6 1.0 HD3 A:ARG342 4.4 9.2 1.0 HD2 A:ARG342 4.4 9.2 1.0 HHC A:HEM502 4.4 7.5 1.0 HHD A:HEM502 4.4 6.0 1.0 HE1 A:PHE297 4.8 10.0 1.0 CD A:ARG342 4.8 7.6 1.0 OD1 A:ASP239 4.9 9.4 1.0 CZ A:ARG342 4.9 6.7 1.0 HD1 A:HIS326 4.9 9.5 1.0

Iron binding site 2 out of 2 in the Dye Type Peroxidase Aa From Streptomyces Lividans with N3 Ligand By Serial Electron Diffraction (Serialed)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Dye Type Peroxidase Aa From Streptomyces Lividans with N3 Ligand By Serial Electron Diffraction (Serialed) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:7.8 occ:1.00 FE B:HEM502 0.0 7.8 1.0 N3 B:AZI501 2.0 13.0 1.0 ND B:HEM502 2.0 7.4 1.0 NB B:HEM502 2.0 8.6 1.0 NC B:HEM502 2.0 8.0 1.0 NA B:HEM502 2.0 7.7 1.0 NE2 B:HIS326 2.2 6.8 1.0 N2 B:AZI501 2.9 22.2 1.0 C1D B:HEM502 3.0 7.7 1.0 C4D B:HEM502 3.0 7.9 1.0 C1B B:HEM502 3.0 9.2 1.0 C4A B:HEM502 3.0 9.1 1.0 C4B B:HEM502 3.0 7.5 1.0 C4C B:HEM502 3.0 9.2 1.0 C1C B:HEM502 3.1 9.1 1.0 C1A B:HEM502 3.1 7.7 1.0 CE1 B:HIS326 3.2 7.6 1.0 CD2 B:HIS326 3.2 9.8 1.0 HE1 B:HIS326 3.3 9.2 1.0 HD2 B:HIS326 3.4 11.7 1.0 CHC B:HEM502 3.4 6.8 1.0 CHD B:HEM502 3.4 6.9 1.0 CHB B:HEM502 3.4 8.9 1.0 CHA B:HEM502 3.4 8.8 1.0 HH11 B:ARG342 3.7 11.9 1.0 N1 B:AZI501 4.0 31.7 1.0 NH1 B:ARG342 4.1 9.9 1.0 C2D B:HEM502 4.2 6.5 1.0 C3D B:HEM502 4.2 7.8 1.0 HH12 B:ARG342 4.2 11.9 1.0 C2B B:HEM502 4.3 7.9 1.0 C3A B:HEM502 4.3 9.8 1.0 C3C B:HEM502 4.3 9.6 1.0 C3B B:HEM502 4.3 9.6 1.0 C2C B:HEM502 4.3 8.1 1.0 C2A B:HEM502 4.3 9.4 1.0 ND1 B:HIS326 4.3 10.1 1.0 CG B:HIS326 4.4 8.0 1.0 HD2 B:ARG342 4.4 11.3 1.0 HHC B:HEM502 4.4 8.2 1.0 HHD B:HEM502 4.4 8.3 1.0 HHB B:HEM502 4.4 10.8 1.0 HHA B:HEM502 4.4 10.6 1.0 HD3 B:ARG342 4.4 11.3 1.0 HE2 B:PHE363 4.6 15.2 1.0 CD B:ARG342 4.8 9.4 1.0 HE1 B:PHE297 4.8 14.9 1.0 CZ B:ARG342 4.8 9.3 1.0 OD1 B:ASP239 5.0 20.9 1.0

G.Hofer, L.Wang, L.Pacoste, P.Hager, A.Fonjallaz, L.Williams, J.Worrall, R.Steiner, H.Xu, X.Zou. Universal Serial Electron Diffraction For High Quality Protein Structures To Be Published.