Iron in PDB 4kn3: Structure of the Y34NS91G Double Mutant of Dehaloperoxidase From Amphitrite Ornata with 2,4,6-Trichlorophenol

The structure of Structure of the Y34NS91G Double Mutant of Dehaloperoxidase From Amphitrite Ornata with 2,4,6-Trichlorophenol, PDB code: 4kn3 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)	44.52 / 1.78
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.982, 67.657, 67.870, 90.00, 90.00, 90.00
R / Rfree (%)	13.3 / 21.4

The structure of Structure of the Y34NS91G Double Mutant of Dehaloperoxidase From Amphitrite Ornata with 2,4,6-Trichlorophenol also contains other interesting chemical elements:

Chlorine

(Cl)

9 atoms

The binding sites of Iron atom in the Structure of the Y34NS91G Double Mutant of Dehaloperoxidase From Amphitrite Ornata with 2,4,6-Trichlorophenol (pdb code 4kn3). 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 Y34NS91G Double Mutant of Dehaloperoxidase From Amphitrite Ornata with 2,4,6-Trichlorophenol, PDB code: 4kn3:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of the Y34NS91G Double Mutant of Dehaloperoxidase 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 Y34NS91G Double Mutant of Dehaloperoxidase From Amphitrite Ornata with 2,4,6-Trichlorophenol within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:33.2 occ:1.00 FE A:HEM201 0.0 33.2 1.0 ND A:HEM201 1.9 32.4 1.0 NA A:HEM201 2.0 30.5 1.0 NC A:HEM201 2.1 33.1 1.0 NB A:HEM201 2.1 25.3 1.0 NE2 A:HIS89 2.4 41.1 1.0 C1D A:HEM201 3.0 39.5 1.0 C4D A:HEM201 3.0 43.1 1.0 C1A A:HEM201 3.0 39.8 1.0 C4C A:HEM201 3.0 31.2 1.0 C1B A:HEM201 3.1 27.4 1.0 C4A A:HEM201 3.1 28.7 1.0 C4B A:HEM201 3.1 25.0 1.0 C1C A:HEM201 3.1 33.1 1.0 CD2 A:HIS89 3.3 53.0 1.0 CL4 A:T6C202 3.3 25.7 0.5 CHD A:HEM201 3.4 38.1 1.0 CHA A:HEM201 3.4 41.6 1.0 CE1 A:HIS89 3.5 51.8 1.0 CHB A:HEM201 3.5 27.4 1.0 CHC A:HEM201 3.5 29.9 1.0 C2A A:HEM201 4.2 36.2 1.0 C2D A:HEM201 4.2 49.9 1.0 C3C A:HEM201 4.3 31.9 1.0 C3A A:HEM201 4.3 30.5 1.0 C3D A:HEM201 4.3 50.3 1.0 C2C A:HEM201 4.3 29.4 1.0 C2B A:HEM201 4.3 24.6 1.0 CG2 A:VAL59 4.3 19.2 1.0 C3B A:HEM201 4.4 28.1 1.0 CG A:HIS89 4.5 51.1 1.0 ND1 A:HIS89 4.5 55.2 1.0 C3 A:T6C202 4.5 19.2 0.5 C4 A:T6C202 4.5 17.9 0.5 O1 A:T6C203 4.6 15.6 0.5 CG1 A:VAL59 4.8 20.6 1.0 CE A:MET86 4.9 43.3 1.0

Iron binding site 2 out of 2 in the Structure of the Y34NS91G Double Mutant of Dehaloperoxidase 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 Y34NS91G Double Mutant of Dehaloperoxidase From Amphitrite Ornata with 2,4,6-Trichlorophenol within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:33.9 occ:1.00 FE B:HEM201 0.0 33.9 1.0 ND B:HEM201 1.9 39.1 1.0 NA B:HEM201 2.0 34.8 1.0 NC B:HEM201 2.1 33.4 1.0 NB B:HEM201 2.1 31.0 1.0 NE2 B:HIS89 2.4 40.1 1.0 C4D B:HEM201 3.0 41.8 1.0 C1D B:HEM201 3.0 37.7 1.0 C1A B:HEM201 3.0 36.9 1.0 C1C B:HEM201 3.1 26.8 1.0 C4B B:HEM201 3.1 29.7 1.0 C4A B:HEM201 3.1 31.2 1.0 C4C B:HEM201 3.1 29.6 1.0 C1B B:HEM201 3.1 30.9 1.0 CD2 B:HIS89 3.3 45.2 1.0 CE1 B:HIS89 3.4 43.2 1.0 CHA B:HEM201 3.4 34.9 1.0 CHC B:HEM201 3.5 28.0 1.0 CHD B:HEM201 3.5 29.1 1.0 CHB B:HEM201 3.5 29.6 1.0 CL4 B:T6C202 3.8 33.4 1.0 CG2 B:VAL59 4.1 19.9 1.0 C2A B:HEM201 4.2 30.2 1.0 C3A B:HEM201 4.2 25.8 1.0 C2D B:HEM201 4.2 40.9 1.0 C2C B:HEM201 4.2 27.9 1.0 C3D B:HEM201 4.3 44.1 1.0 C3C B:HEM201 4.3 30.2 1.0 C2B B:HEM201 4.3 27.0 1.0 C3B B:HEM201 4.4 27.5 1.0 CG B:HIS89 4.4 42.3 1.0 ND1 B:HIS89 4.5 37.7 1.0 C3 B:T6C202 4.6 38.1 1.0 C4 B:T6C202 4.7 26.1 1.0 CE B:MET86 4.7 35.8 1.0 CG1 B:VAL59 5.0 20.8 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