Iron in PDB 3ok5: Structure of the H55D Mutant of Dehaloperoxidase-Hemoglobin A From Amphitriti Ornata with 4-Bromophenol Inhibitor

The structure of Structure of the H55D Mutant of Dehaloperoxidase-Hemoglobin A From Amphitriti Ornata with 4-Bromophenol Inhibitor, PDB code: 3ok5 was solved by J.Zhao, V.S.De Serrano, S.Franzen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 1.72
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.055, 67.600, 68.490, 90.00, 90.00, 90.00
R / Rfree (%)	24.1 / 29.7

The structure of Structure of the H55D Mutant of Dehaloperoxidase-Hemoglobin A From Amphitriti Ornata with 4-Bromophenol Inhibitor also contains other interesting chemical elements:

Bromine

(Br)

4 atoms

The binding sites of Iron atom in the Structure of the H55D Mutant of Dehaloperoxidase-Hemoglobin A From Amphitriti Ornata with 4-Bromophenol Inhibitor (pdb code 3ok5). 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 the H55D Mutant of Dehaloperoxidase-Hemoglobin A From Amphitriti Ornata with 4-Bromophenol Inhibitor, PDB code: 3ok5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of the H55D Mutant of Dehaloperoxidase-Hemoglobin A From Amphitriti Ornata with 4-Bromophenol Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the H55D Mutant of Dehaloperoxidase-Hemoglobin A From Amphitriti Ornata with 4-Bromophenol Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe139 b:13.6 occ:1.00 FE A:HEM139 0.0 13.6 1.0 ND A:HEM139 2.0 15.3 1.0 NA A:HEM139 2.1 14.5 1.0 NC A:HEM139 2.1 13.7 1.0 NB A:HEM139 2.1 12.4 1.0 NE2 A:HIS89 2.1 20.0 1.0 C1D A:HEM139 3.0 16.5 1.0 C4D A:HEM139 3.1 17.3 1.0 C4A A:HEM139 3.1 13.9 1.0 C4C A:HEM139 3.1 13.9 1.0 C1A A:HEM139 3.1 16.1 1.0 CD2 A:HIS89 3.1 20.4 1.0 C4B A:HEM139 3.1 11.2 1.0 C1B A:HEM139 3.1 12.1 1.0 C1C A:HEM139 3.1 12.9 1.0 CE1 A:HIS89 3.1 19.4 1.0 CHD A:HEM139 3.4 15.3 1.0 CHA A:HEM139 3.4 16.6 1.0 CHB A:HEM139 3.5 12.7 1.0 CHC A:HEM139 3.5 12.3 1.0 C5 A:BML138 3.5 16.8 0.2 C6 A:BML138 3.8 16.8 0.2 ND1 A:HIS89 4.2 20.4 1.0 CG A:HIS89 4.3 20.7 1.0 C2D A:HEM139 4.3 17.3 1.0 C3D A:HEM139 4.3 17.9 1.0 C3A A:HEM139 4.3 15.0 1.0 C2A A:HEM139 4.3 15.5 1.0 C3C A:HEM139 4.3 14.1 1.0 C3B A:HEM139 4.3 11.5 1.0 C2C A:HEM139 4.3 12.4 1.0 C2B A:HEM139 4.3 11.1 1.0 CG2 A:VAL59 4.3 8.8 1.0 C5 A:BML138 4.4 11.5 0.2 BR4 A:BML138 4.4 13.4 0.2 C4 A:BML138 4.5 17.1 0.2 C4 A:BML138 4.7 11.6 0.2 CE A:MET86 4.8 18.8 0.5 CG1 A:VAL59 4.8 8.5 1.0

Iron binding site 2 out of 2 in the Structure of the H55D Mutant of Dehaloperoxidase-Hemoglobin A From Amphitriti Ornata with 4-Bromophenol Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the H55D Mutant of Dehaloperoxidase-Hemoglobin A From Amphitriti Ornata with 4-Bromophenol Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe139 b:6.6 occ:1.00 FE B:HEM139 0.0 6.6 1.0 NA B:HEM139 2.0 6.9 1.0 NB B:HEM139 2.1 5.8 1.0 NC B:HEM139 2.1 5.8 1.0 ND B:HEM139 2.1 6.6 1.0 NE2 B:HIS89 2.2 9.4 1.0 C4A B:HEM139 3.0 6.4 1.0 C4B B:HEM139 3.1 4.5 1.0 C1A B:HEM139 3.1 8.4 1.0 C1B B:HEM139 3.1 5.5 1.0 C1C B:HEM139 3.1 4.9 1.0 C4D B:HEM139 3.1 7.2 1.0 C4C B:HEM139 3.1 5.5 1.0 C1D B:HEM139 3.1 7.7 1.0 CE1 B:HIS89 3.1 8.7 1.0 CD2 B:HIS89 3.2 9.4 1.0 CHB B:HEM139 3.4 5.3 1.0 CHC B:HEM139 3.4 2.0 1.0 CHA B:HEM139 3.4 7.9 1.0 CHD B:HEM139 3.5 6.9 1.0 C5 B:BML138 3.8 80.0 0.4 CG2 B:VAL59 4.0 6.9 1.0 C6 B:BML138 4.0 79.9 0.4 C3A B:HEM139 4.2 7.2 1.0 C2A B:HEM139 4.3 9.6 1.0 ND1 B:HIS89 4.3 9.9 1.0 C3B B:HEM139 4.3 4.6 1.0 C2B B:HEM139 4.3 4.2 1.0 C2C B:HEM139 4.3 4.8 1.0 C3C B:HEM139 4.3 6.5 1.0 C3D B:HEM139 4.3 8.0 1.0 CG B:HIS89 4.3 10.4 1.0 C2D B:HEM139 4.3 8.9 1.0 C5 B:BML138 4.6 20.4 0.2 CE B:MET86 4.6 11.8 1.0 C4 B:BML138 4.8 80.0 0.4 CG1 B:VAL59 4.8 5.8 1.0

J.Zhao, V.S.De Serrano, S.Franzen. Effect of the H55D Mutation on the Kinetics and Structure of Dehaloperoxidase-Hemoglobin A To Be Published.