Iron in PDB 5vrt: Nonheme Iron Replacement in A Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Co-Bound Febmb

The structure of Nonheme Iron Replacement in A Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Co-Bound Febmb, PDB code: 5vrt was solved by J.Reed, Y.Shi, Q.Zhu, S.Chakraborty, E.N.Mirs, I.D.Petrik, A.Bhagi-Damodaran, M.Ross, P.Moenne-Loccoz, Y.Zhang, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.16 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.657, 47.328, 76.056, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 23.9

The structure of Nonheme Iron Replacement in A Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Co-Bound Febmb also contains other interesting chemical elements:

Cobalt

(Co)

1 atom

The binding sites of Iron atom in the Nonheme Iron Replacement in A Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Co-Bound Febmb (pdb code 5vrt). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Nonheme Iron Replacement in A Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Co-Bound Febmb, PDB code: 5vrt:

Iron binding site 1 out of 1 in the Nonheme Iron Replacement in A Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Co-Bound Febmb


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Nonheme Iron Replacement in A Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Co-Bound Febmb within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:23.5 occ:1.00 FE A:HEM201 0.0 23.5 1.0 NA A:HEM201 2.0 25.0 1.0 NC A:HEM201 2.0 26.4 1.0 NB A:HEM201 2.0 22.0 1.0 ND A:HEM201 2.0 26.2 1.0 NE2 A:HIS93 2.3 25.2 1.0 OE1 A:GLU68 2.5 23.6 1.0 C4D A:HEM201 3.0 30.1 1.0 C4C A:HEM201 3.0 25.1 1.0 C1B A:HEM201 3.0 19.8 1.0 C1C A:HEM201 3.0 22.4 1.0 C1A A:HEM201 3.0 30.2 1.0 C4A A:HEM201 3.0 24.9 1.0 C4B A:HEM201 3.1 20.9 1.0 C1D A:HEM201 3.1 27.8 1.0 CE1 A:HIS93 3.1 33.9 1.0 CD2 A:HIS93 3.4 22.9 1.0 CD A:GLU68 3.4 19.6 1.0 CHA A:HEM201 3.5 32.0 1.0 CHB A:HEM201 3.5 20.6 1.0 CHC A:HEM201 3.5 22.1 1.0 CHD A:HEM201 3.5 26.1 1.0 CG A:GLU68 3.8 24.9 1.0 C3C A:HEM201 4.2 24.5 1.0 C3D A:HEM201 4.2 32.5 1.0 C2B A:HEM201 4.2 21.1 1.0 C3B A:HEM201 4.2 22.3 1.0 C2A A:HEM201 4.3 32.1 1.0 C3A A:HEM201 4.3 24.6 1.0 C2C A:HEM201 4.3 24.0 1.0 C2D A:HEM201 4.3 35.8 1.0 ND1 A:HIS93 4.3 26.9 1.0 CE1 A:HIS64 4.4 25.9 1.0 CG A:HIS93 4.4 24.7 1.0 OE2 A:GLU68 4.5 25.0 1.0 CO A:CO202 4.6 19.1 1.0 CB A:GLU68 4.9 16.6 1.0 O A:HOH335 4.9 23.2 1.0 NE2 A:HIS64 5.0 23.6 1.0

J.H.Reed, Y.Shi, Q.Zhu, S.Chakraborty, E.N.Mirts, I.D.Petrik, A.Bhagi-Damodaran, M.Ross, P.Moenne-Loccoz, Y.Zhang, Y.Lu. Manganese and Cobalt in the Nonheme-Metal-Binding Site of A Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity Through Redox-Inactive Mechanism. J. Am. Chem. Soc. V. 139 12209 2017.
ISSN: ESSN 1520-5126
PubMed: 28768416
DOI: 10.1021/JACS.7B05800