Iron in PDB 4kmw: Structure of the Y34N Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol

The structure of Structure of the Y34N Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol, PDB code: 4kmw was solved by C.Wang, L.Lovelace, L.Lebioda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.78 / 1.79
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.553, 67.259, 67.890, 90.00, 90.00, 90.00
R / Rfree (%)	14.6 / 23.2

The structure of Structure of the Y34N Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol also contains other interesting chemical elements:

Chlorine

(Cl)

6 atoms

The binding sites of Iron atom in the Structure of the Y34N Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol (pdb code 4kmw). 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 Y34N Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol, PDB code: 4kmw:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of the Y34N Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol


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 Y34N Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:41.6 occ:1.00 FE A:HEM201 0.0 41.6 1.0 ND A:HEM201 1.9 45.0 1.0 NA A:HEM201 2.0 34.9 1.0 NC A:HEM201 2.1 40.6 1.0 NB A:HEM201 2.1 33.0 1.0 NE2 A:HIS89 2.4 47.0 1.0 C1D A:HEM201 2.9 44.4 1.0 C4D A:HEM201 3.0 53.4 1.0 C1A A:HEM201 3.0 46.0 1.0 C4C A:HEM201 3.0 42.9 1.0 C4A A:HEM201 3.1 37.3 1.0 C1B A:HEM201 3.1 35.9 1.0 C1C A:HEM201 3.1 39.1 1.0 C4B A:HEM201 3.1 27.6 1.0 CL4 A:T6C202 3.3 39.4 1.0 CD2 A:HIS89 3.3 57.1 1.0 CE1 A:HIS89 3.4 51.2 1.0 CHD A:HEM201 3.4 37.3 1.0 CHA A:HEM201 3.4 54.8 1.0 CHB A:HEM201 3.5 29.9 1.0 CHC A:HEM201 3.5 35.4 1.0 C2A A:HEM201 4.2 45.0 1.0 C2D A:HEM201 4.2 48.0 1.0 CG2 A:VAL59 4.2 23.5 1.0 C3D A:HEM201 4.3 51.9 1.0 C3C A:HEM201 4.3 41.0 1.0 C2C A:HEM201 4.3 32.4 1.0 C3A A:HEM201 4.3 40.4 1.0 C2B A:HEM201 4.3 33.0 1.0 C3B A:HEM201 4.4 29.6 1.0 C3 A:T6C202 4.4 40.5 1.0 C4 A:T6C202 4.4 37.0 1.0 ND1 A:HIS89 4.5 41.1 1.0 CG A:HIS89 4.5 53.0 1.0 CE A:MET86 4.7 50.1 1.0 CG1 A:VAL59 4.8 20.8 1.0

Iron binding site 2 out of 2 in the Structure of the Y34N Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol


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 Y34N Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:32.8 occ:1.00 FE B:HEM201 0.0 32.8 1.0 ND B:HEM201 1.9 37.6 1.0 NA B:HEM201 2.0 34.3 1.0 NC B:HEM201 2.1 29.4 1.0 NB B:HEM201 2.1 28.8 1.0 NE2 B:HIS89 2.4 33.9 1.0 C1D B:HEM201 2.9 34.4 1.0 C4D B:HEM201 2.9 35.8 1.0 C1A B:HEM201 3.0 36.6 1.0 C4A B:HEM201 3.0 32.9 1.0 C4B B:HEM201 3.1 23.6 1.0 C4C B:HEM201 3.1 28.1 1.0 C1C B:HEM201 3.1 26.4 1.0 C1B B:HEM201 3.1 30.0 1.0 CE1 B:HIS89 3.3 34.9 1.0 CD2 B:HIS89 3.3 40.0 1.0 CHA B:HEM201 3.4 35.1 1.0 CHD B:HEM201 3.4 29.5 1.0 CHB B:HEM201 3.4 31.5 1.0 CHC B:HEM201 3.5 27.7 1.0 CL4 B:T6C202 3.8 34.6 1.0 CG2 B:VAL59 4.1 26.5 1.0 C2A B:HEM201 4.2 37.5 1.0 C2D B:HEM201 4.2 37.1 1.0 C3A B:HEM201 4.2 35.1 1.0 C3D B:HEM201 4.2 35.3 1.0 C3C B:HEM201 4.3 27.3 1.0 C2C B:HEM201 4.3 27.0 1.0 C2B B:HEM201 4.4 24.2 1.0 C3B B:HEM201 4.4 25.9 1.0 ND1 B:HIS89 4.4 28.4 1.0 CG B:HIS89 4.5 38.0 1.0 C3 B:T6C202 4.7 51.0 1.0 CE B:MET86 4.8 32.6 1.0 C4 B:T6C202 4.8 36.7 1.0

C.Wang, L.L.Lovelace, S.Sun, J.H.Dawson, L.Lebioda. Complexes of Dual-Function Hemoglobin/Dehaloperoxidase with Substrate 2,4,6-Trichlorophenol Are Inhibitory and Indicate Binding of Halophenol to Compound I. Biochemistry V. 52 6203 2013.
ISSN: ISSN 0006-2960
PubMed: 23952341
DOI: 10.1021/BI400627W