Iron in PDB 5vlx: Dehaloperoxidase B Mutant F21W

The structure of Dehaloperoxidase B Mutant F21W, PDB code: 5vlx was solved by L.M.Carey, R.A.Ghiladi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.69 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.479, 67.130, 67.368, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 20.4

The binding sites of Iron atom in the Dehaloperoxidase B Mutant F21W (pdb code 5vlx). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Dehaloperoxidase B Mutant F21W, PDB code: 5vlx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Dehaloperoxidase B Mutant F21W


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Dehaloperoxidase B Mutant F21W within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:22.1 occ:1.00 FE A:HEM201 0.0 22.1 1.0 NC A:HEM201 2.0 17.7 1.0 NA A:HEM201 2.0 19.9 1.0 ND A:HEM201 2.1 24.5 1.0 NB A:HEM201 2.1 17.0 1.0 NE2 A:HIS89 2.3 19.5 1.0 C4C A:HEM201 3.0 23.7 1.0 C1D A:HEM201 3.1 26.2 1.0 C1C A:HEM201 3.1 17.6 1.0 C4A A:HEM201 3.1 15.2 1.0 C1A A:HEM201 3.1 19.1 1.0 C4B A:HEM201 3.1 19.3 1.0 C1B A:HEM201 3.1 14.8 1.0 C4D A:HEM201 3.1 24.8 1.0 CD2 A:HIS89 3.2 24.8 1.0 CE1 A:HIS89 3.3 20.0 1.0 CHD A:HEM201 3.4 24.3 1.0 CHC A:HEM201 3.4 20.2 1.0 CHB A:HEM201 3.5 15.1 1.0 CHA A:HEM201 3.5 17.0 1.0 C3C A:HEM201 4.2 22.3 1.0 C2C A:HEM201 4.3 17.8 1.0 C3A A:HEM201 4.3 19.4 1.0 C2A A:HEM201 4.3 17.7 1.0 C2D A:HEM201 4.3 22.9 1.0 CG2 A:VAL59 4.3 14.6 1.0 C3D A:HEM201 4.3 20.3 1.0 C3B A:HEM201 4.3 17.9 1.0 C2B A:HEM201 4.3 15.8 1.0 ND1 A:HIS89 4.4 19.7 1.0 CG A:HIS89 4.4 22.6 1.0 CE A:MET86 4.7 20.4 1.0 O A:HOH354 4.8 24.3 1.0 CG1 A:VAL59 4.9 15.5 1.0

Iron binding site 2 out of 2 in the Dehaloperoxidase B Mutant F21W


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Dehaloperoxidase B Mutant F21W 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 NC B:HEM201 2.0 18.2 1.0 NA B:HEM201 2.0 19.1 1.0 ND B:HEM201 2.0 20.2 1.0 NB B:HEM201 2.1 17.7 1.0 NE2 B:HIS89 2.3 24.5 1.0 C4C B:HEM201 3.0 20.9 1.0 C1A B:HEM201 3.0 20.8 1.0 C4A B:HEM201 3.0 19.3 1.0 C1C B:HEM201 3.0 18.9 1.0 C4D B:HEM201 3.1 28.9 1.0 C1D B:HEM201 3.1 23.0 1.0 C1B B:HEM201 3.1 18.3 1.0 C4B B:HEM201 3.1 20.7 1.0 CD2 B:HIS89 3.2 21.2 1.0 CE1 B:HIS89 3.3 21.3 1.0 CHB B:HEM201 3.4 18.0 1.0 CHA B:HEM201 3.4 23.8 1.0 CHD B:HEM201 3.4 21.6 1.0 CHC B:HEM201 3.5 21.7 1.0 C3C B:HEM201 4.2 19.1 1.0 C2A B:HEM201 4.3 20.1 1.0 C2C B:HEM201 4.3 15.3 1.0 C3A B:HEM201 4.3 18.9 1.0 CG2 B:VAL59 4.3 19.8 1.0 C3D B:HEM201 4.3 26.1 1.0 C2D B:HEM201 4.3 23.3 1.0 C2B B:HEM201 4.3 18.5 1.0 C3B B:HEM201 4.3 18.8 1.0 ND1 B:HIS89 4.4 21.7 1.0 CG B:HIS89 4.4 24.0 1.0 CE B:MET86 4.6 23.3 1.0 O B:HOH351 4.9 32.0 1.0 CG1 B:VAL59 4.9 15.1 1.0

L.M.Carey, K.B.Kim, N.L.Mccombs, P.Swartz, C.Kim, R.A.Ghiladi. Selective Tuning of Activity in A Multifunctional Enzyme As Revealed in the F21W Mutant of Dehaloperoxidase B From Amphitrite Ornata. J. Biol. Inorg. Chem. V. 23 209 2018.
ISSN: ESSN 1432-1327
PubMed: 29170897
DOI: 10.1007/S00775-017-1520-X