Iron in PDB 1df1: Murine Inosoxy Dimer with Isothiourea Bound in the Active Site

All present enzymatic activity of Murine Inosoxy Dimer with Isothiourea Bound in the Active Site:
1.14.13.39;

The structure of Murine Inosoxy Dimer with Isothiourea Bound in the Active Site, PDB code: 1df1 was solved by B.R.Crane, R.J.Rosenfeld, A.S.Arvai, D.K.Ghosh, S.Ghosh, J.A.Tainer, D.J.Stuehr, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.35
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	214.464, 214.464, 112.752, 90.00, 90.00, 120.00
R / Rfree (%)	22.3 / 29.8

The structure of Murine Inosoxy Dimer with Isothiourea Bound in the Active Site also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Murine Inosoxy Dimer with Isothiourea Bound in the Active Site (pdb code 1df1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Murine Inosoxy Dimer with Isothiourea Bound in the Active Site, PDB code: 1df1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Murine Inosoxy Dimer with Isothiourea Bound in the Active Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Murine Inosoxy Dimer with Isothiourea Bound in the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:28.0 occ:1.00 FE A:HEM901 0.0 28.0 1.0 NA A:HEM901 1.9 20.4 1.0 NB A:HEM901 2.0 22.2 1.0 NC A:HEM901 2.1 24.2 1.0 ND A:HEM901 2.1 20.5 1.0 SG A:CYS194 2.5 30.9 1.0 C1B A:HEM901 3.0 21.3 1.0 C4A A:HEM901 3.0 22.5 1.0 C4B A:HEM901 3.0 23.5 1.0 C1A A:HEM901 3.0 25.5 1.0 C1C A:HEM901 3.1 27.8 1.0 C4C A:HEM901 3.1 24.2 1.0 C4D A:HEM901 3.1 22.8 1.0 C1D A:HEM901 3.2 20.3 1.0 CHB A:HEM901 3.4 19.6 1.0 CB A:CYS194 3.4 21.8 1.0 CHC A:HEM901 3.4 25.7 1.0 CHA A:HEM901 3.4 22.3 1.0 CHD A:HEM901 3.5 25.9 1.0 S A:ITU899 3.8 34.9 1.0 C2 A:ITU899 4.0 27.0 1.0 CA A:CYS194 4.1 28.5 1.0 C2B A:HEM901 4.2 19.7 1.0 C3B A:HEM901 4.2 17.6 1.0 C3A A:HEM901 4.3 24.1 1.0 C2A A:HEM901 4.3 22.0 1.0 C2C A:HEM901 4.3 25.5 1.0 C3C A:HEM901 4.4 27.0 1.0 NE1 A:TRP188 4.4 34.7 1.0 C3D A:HEM901 4.4 20.9 1.0 C1 A:ITU899 4.4 22.4 1.0 C2D A:HEM901 4.5 18.9 1.0 C3 A:ITU899 4.6 23.1 1.0 N A:GLY196 4.7 32.0 1.0 N A:ILE195 4.8 34.3 1.0 C A:CYS194 4.8 31.9 1.0 N1 A:ITU899 4.9 24.9 1.0

Iron binding site 2 out of 2 in the Murine Inosoxy Dimer with Isothiourea Bound in the Active Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Murine Inosoxy Dimer with Isothiourea Bound in the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:28.4 occ:1.00 FE B:HEM901 0.0 28.4 1.0 NA B:HEM901 2.0 21.0 1.0 NB B:HEM901 2.0 22.5 1.0 NC B:HEM901 2.0 27.5 1.0 ND B:HEM901 2.1 23.3 1.0 SG B:CYS194 2.4 32.0 1.0 C4B B:HEM901 3.0 23.5 1.0 C1A B:HEM901 3.0 25.1 1.0 C4A B:HEM901 3.0 21.8 1.0 C1C B:HEM901 3.0 29.6 1.0 C1B B:HEM901 3.0 20.1 1.0 C4C B:HEM901 3.1 27.4 1.0 C4D B:HEM901 3.1 20.4 1.0 C1D B:HEM901 3.1 22.0 1.0 CB B:CYS194 3.3 23.4 1.0 CHC B:HEM901 3.4 25.0 1.0 CHB B:HEM901 3.4 18.9 1.0 CHA B:HEM901 3.5 23.2 1.0 CHD B:HEM901 3.5 25.0 1.0 S B:ITU1899 3.9 33.3 1.0 CA B:CYS194 4.0 31.5 1.0 C2 B:ITU1899 4.2 39.0 1.0 C3B B:HEM901 4.3 22.7 1.0 C2B B:HEM901 4.3 22.2 1.0 C3A B:HEM901 4.3 21.6 1.0 C2A B:HEM901 4.3 22.8 1.0 C2C B:HEM901 4.3 26.1 1.0 NE1 B:TRP188 4.3 22.8 1.0 C3D B:HEM901 4.3 21.3 1.0 C3C B:HEM901 4.4 26.1 1.0 C1 B:ITU1899 4.4 35.5 1.0 C2D B:HEM901 4.4 21.4 1.0 O B:HOH1123 4.5 97.3 1.0 O B:HOH1125 4.6 73.5 1.0 C3 B:ITU1899 4.7 26.5 1.0 N B:GLY196 4.8 31.2 1.0 C B:CYS194 4.8 35.4 1.0 N B:ILE195 4.9 36.1 1.0 CD1 B:TRP188 4.9 23.0 1.0

B.R.Crane, R.J.Rosenfeld, A.S.Arvai, D.K.Ghosh, S.Ghosh, J.A.Tainer, D.J.Stuehr, E.D.Getzoff. N-Terminal Domain Swapping and Metal Ion Binding in Nitric Oxide Synthase Dimerization. Embo J. V. 18 6271 1999.
ISSN: ISSN 0261-4189
PubMed: 10562539
DOI: 10.1093/EMBOJ/18.22.6271