Iron in PDB 4hsx: Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol

All present enzymatic activity of Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol:
1.11.1.7;

The structure of Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol, PDB code: 4hsx was solved by M.K.Thompson, A.Plummer, S.Franzen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.34 / 1.12
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.241, 67.441, 69.338, 90.00, 90.00, 90.00
R / Rfree (%)	12.6 / 15

The structure of Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol also contains other interesting chemical elements:

Bromine

(Br)

2 atoms

The binding sites of Iron atom in the Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol (pdb code 4hsx). 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 L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol, PDB code: 4hsx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol


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 L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:7.7 occ:1.00 FE A:HEM201 0.0 7.7 1.0 ND A:HEM201 2.0 7.3 1.0 NA A:HEM201 2.0 7.2 1.0 NC A:HEM201 2.0 7.9 1.0 NB A:HEM201 2.1 7.3 1.0 NE2 A:HIS89 2.1 7.3 1.0 O A:HOH512 2.2 12.9 1.0 C1D A:HEM201 3.0 8.2 1.0 C4D A:HEM201 3.0 7.9 1.0 C4C A:HEM201 3.1 8.4 1.0 CE1 A:HIS89 3.1 8.7 1.0 C1C A:HEM201 3.1 8.6 1.0 C1B A:HEM201 3.1 7.0 1.0 C4B A:HEM201 3.1 7.5 1.0 C1A A:HEM201 3.1 7.2 1.0 C4A A:HEM201 3.1 7.5 1.0 CD2 A:HIS89 3.1 9.1 1.0 CHC A:HEM201 3.4 7.9 1.0 CHD A:HEM201 3.4 8.8 1.0 CHA A:HEM201 3.4 7.9 1.0 CHB A:HEM201 3.4 7.4 1.0 C3 A:BML206 3.7 6.6 0.3 ND1 A:HIS89 4.2 8.3 1.0 C2D A:HEM201 4.3 9.3 1.0 CG A:HIS89 4.3 8.0 1.0 C2C A:HEM201 4.3 9.6 1.0 C3C A:HEM201 4.3 9.9 1.0 C3D A:HEM201 4.3 9.6 1.0 C3B A:HEM201 4.3 8.0 1.0 C3A A:HEM201 4.3 7.7 1.0 C2A A:HEM201 4.3 7.5 1.0 C2B A:HEM201 4.3 7.8 1.0 C4 A:BML206 4.4 6.4 0.3 CG2 A:VAL59 4.5 8.7 1.0 C2 A:BML206 4.5 8.6 0.3 BR4 A:BML206 4.6 12.0 0.3 NE2 A:HIS55 4.6 7.9 0.4 CE A:MET86 4.8 11.2 1.0

Iron binding site 2 out of 2 in the Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol


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 L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:8.1 occ:1.00 FE B:HEM201 0.0 8.1 1.0 NC B:HEM201 2.0 8.6 1.0 NA B:HEM201 2.0 7.7 1.0 ND B:HEM201 2.1 8.2 1.0 NB B:HEM201 2.1 7.7 1.0 NE2 B:HIS89 2.1 7.5 1.0 O B:HOH494 2.3 10.1 0.5 C1A B:HEM201 3.0 7.2 1.0 C4C B:HEM201 3.1 9.7 1.0 C4D B:HEM201 3.1 8.3 1.0 C1D B:HEM201 3.1 8.6 1.0 C1C B:HEM201 3.1 8.7 1.0 CE1 B:HIS89 3.1 8.8 1.0 C1B B:HEM201 3.1 8.0 1.0 C4A B:HEM201 3.1 7.4 1.0 C4B B:HEM201 3.1 8.0 1.0 CD2 B:HIS89 3.1 8.6 1.0 CHC B:HEM201 3.4 9.9 1.0 CHD B:HEM201 3.4 9.9 1.0 CHA B:HEM201 3.4 7.7 1.0 CHB B:HEM201 3.5 7.8 1.0 C3 B:BML203 3.9 8.3 0.4 C2 B:BML203 4.1 7.5 0.4 ND1 B:HIS89 4.2 7.7 1.0 CG B:HIS89 4.3 7.7 1.0 C3B B:HEM201 4.3 8.6 1.0 C2A B:HEM201 4.3 8.3 1.0 C3A B:HEM201 4.3 7.6 1.0 C2D B:HEM201 4.3 10.3 1.0 C3C B:HEM201 4.3 10.6 1.0 C3D B:HEM201 4.3 10.0 1.0 C2C B:HEM201 4.3 10.4 1.0 C2B B:HEM201 4.3 8.4 1.0 CG2 B:VAL59 4.4 8.7 1.0 C4 B:BML203 4.7 7.9 0.4 CE B:MET86 4.7 11.3 1.0 CG1 B:VAL59 5.0 7.2 1.0

A.Plummer, M.K.Thompson, S.Franzen. Role of Polarity of the Distal Pocket in the Control of Inhibitor Binding in Dehaloperoxidase-Hemoglobin. Biochemistry V. 52 2218 2013.
ISSN: ISSN 0006-2960
PubMed: 23480794
DOI: 10.1021/BI301509R