Iron in PDB 4kmv: Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol

The structure of Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol, PDB code: 4kmv 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)	37.21 / 1.44
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.539, 67.804, 68.368, 90.00, 90.00, 90.00
R / Rfree (%)	13.3 / 20.1

The structure of Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Iron atom in the Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 2,4,6-Trichlorophenol (pdb code 4kmv). 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 2,4,6-Trichlorophenol, PDB code: 4kmv:
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 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 L100F 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:20.5 occ:1.00 FE A:HEM201 0.0 20.5 1.0 ND A:HEM201 1.9 19.9 1.0 NA A:HEM201 2.0 19.5 1.0 NC A:HEM201 2.1 19.2 1.0 NB A:HEM201 2.1 16.1 1.0 O A:HOH301 2.1 25.1 0.5 NE2 A:HIS89 2.1 24.2 1.0 O1 A:OXY202 2.5 28.6 0.5 C1D A:HEM201 3.0 20.2 1.0 C4D A:HEM201 3.0 21.6 1.0 C1A A:HEM201 3.0 20.7 1.0 C4B A:HEM201 3.0 18.5 1.0 C4C A:HEM201 3.1 20.4 1.0 C4A A:HEM201 3.1 19.4 1.0 CE1 A:HIS89 3.1 22.1 1.0 C1C A:HEM201 3.1 18.3 1.0 C1B A:HEM201 3.1 17.5 1.0 CD2 A:HIS89 3.1 25.2 1.0 CHD A:HEM201 3.4 21.4 1.0 CHA A:HEM201 3.4 18.7 1.0 CHC A:HEM201 3.4 20.8 1.0 CHB A:HEM201 3.5 19.5 1.0 O2 A:OXY202 3.7 39.9 0.5 ND1 A:HIS89 4.2 21.3 1.0 C2A A:HEM201 4.2 20.7 1.0 C3D A:HEM201 4.3 23.4 1.0 CG A:HIS89 4.3 25.0 1.0 C2D A:HEM201 4.3 22.6 1.0 C3A A:HEM201 4.3 18.1 1.0 C3C A:HEM201 4.3 21.1 1.0 C2C A:HEM201 4.3 22.4 1.0 C2B A:HEM201 4.3 18.5 1.0 C3B A:HEM201 4.3 17.5 1.0 CG2 A:VAL59 4.5 18.9 1.0 O1 A:T6C203 4.6 24.8 0.5 CE A:MET86 4.6 20.1 0.5 CE1 A:HIS55 4.9 20.5 0.6

Iron binding site 2 out of 2 in the Structure of the L100F 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 L100F 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:21.8 occ:1.00 FE B:HEM201 0.0 21.8 1.0 ND B:HEM201 1.9 22.9 1.0 NA B:HEM201 2.0 23.7 1.0 NB B:HEM201 2.1 19.6 1.0 NC B:HEM201 2.1 24.4 1.0 NE2 B:HIS89 2.2 19.9 1.0 O B:HOH301 2.7 34.9 1.0 C1D B:HEM201 3.0 23.9 1.0 C4D B:HEM201 3.0 21.1 1.0 C1B B:HEM201 3.0 19.3 1.0 C4B B:HEM201 3.0 21.5 1.0 C1A B:HEM201 3.1 22.3 1.0 C4C B:HEM201 3.1 25.2 1.0 C4A B:HEM201 3.1 21.9 1.0 C1C B:HEM201 3.1 21.1 1.0 CE1 B:HIS89 3.2 25.0 1.0 CD2 B:HIS89 3.2 21.7 1.0 CHC B:HEM201 3.4 20.2 1.0 CHA B:HEM201 3.4 24.1 1.0 CHD B:HEM201 3.4 23.8 1.0 CHB B:HEM201 3.4 21.9 1.0 C3D B:HEM201 4.3 24.0 1.0 C2D B:HEM201 4.3 26.6 1.0 C2B B:HEM201 4.3 19.8 1.0 C2A B:HEM201 4.3 21.1 1.0 C3C B:HEM201 4.3 23.3 1.0 ND1 B:HIS89 4.3 23.2 1.0 C2C B:HEM201 4.3 21.4 1.0 C3A B:HEM201 4.3 21.0 1.0 C3B B:HEM201 4.3 20.4 1.0 CG2 B:VAL59 4.3 17.8 1.0 O1 B:EDO202 4.3 37.0 1.0 CG B:HIS89 4.3 21.0 1.0 CE B:MET86 4.8 27.1 1.0 CG1 B:VAL59 5.0 17.5 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