Iron in PDB 1qom: Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Swapped N-Terminal Hook

All present enzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Swapped N-Terminal Hook:
1.14.13.39;

The structure of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Swapped N-Terminal Hook, PDB code: 1qom was solved by B.R.Crane, R.A.Rosenfeld, A.S.Arvai, 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 / 2.70
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	212.980, 212.980, 114.200, 90.00, 90.00, 120.00
R / Rfree (%)	23.6 / 30.6

The binding sites of Iron atom in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Swapped N-Terminal Hook (pdb code 1qom). 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 Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Swapped N-Terminal Hook, PDB code: 1qom:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Swapped N-Terminal Hook


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Swapped N-Terminal Hook within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:50.6 occ:1.00 FE A:HEM901 0.0 50.6 1.0 ND A:HEM901 2.0 52.6 1.0 NC A:HEM901 2.0 44.9 1.0 NA A:HEM901 2.0 47.7 1.0 NB A:HEM901 2.0 45.7 1.0 SG A:CYS194 2.3 56.2 1.0 C1D A:HEM901 3.0 53.3 1.0 C4C A:HEM901 3.0 49.6 1.0 C1A A:HEM901 3.0 50.7 1.0 C1C A:HEM901 3.0 49.4 1.0 C4A A:HEM901 3.0 50.7 1.0 C4D A:HEM901 3.0 54.0 1.0 C1B A:HEM901 3.1 45.6 1.0 C4B A:HEM901 3.1 47.5 1.0 CB A:CYS194 3.3 54.3 1.0 CHD A:HEM901 3.4 51.3 1.0 CHA A:HEM901 3.4 53.2 1.0 CHB A:HEM901 3.4 48.9 1.0 CHC A:HEM901 3.4 45.3 1.0 O A:HOH2188 3.4 23.9 1.0 CA A:CYS194 4.1 51.5 1.0 C2A A:HEM901 4.2 47.0 1.0 C3D A:HEM901 4.3 47.9 1.0 C3A A:HEM901 4.3 47.9 1.0 C2D A:HEM901 4.3 49.9 1.0 C2C A:HEM901 4.3 53.4 1.0 C3C A:HEM901 4.3 53.0 1.0 C2B A:HEM901 4.3 45.4 1.0 C3B A:HEM901 4.3 48.4 1.0 NE1 A:TRP188 4.4 59.5 1.0 N A:ILE195 4.9 50.4 1.0 N A:GLY196 4.9 42.2 1.0 C A:CYS194 4.9 51.3 1.0

Iron binding site 2 out of 2 in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Swapped N-Terminal Hook


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Swapped N-Terminal Hook within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:44.3 occ:1.00 FE B:HEM901 0.0 44.3 1.0 NC B:HEM901 2.0 53.6 1.0 ND B:HEM901 2.0 46.8 1.0 NA B:HEM901 2.0 44.1 1.0 NB B:HEM901 2.0 48.7 1.0 SG B:CYS194 2.4 45.5 1.0 C1A B:HEM901 3.0 44.9 1.0 C1C B:HEM901 3.0 53.8 1.0 C4D B:HEM901 3.0 49.4 1.0 C1D B:HEM901 3.0 50.8 1.0 C4C B:HEM901 3.0 55.3 1.0 C4A B:HEM901 3.0 47.1 1.0 C1B B:HEM901 3.1 48.9 1.0 C4B B:HEM901 3.1 49.9 1.0 O B:HOH2200 3.2 31.9 1.0 CB B:CYS194 3.3 50.1 1.0 CHA B:HEM901 3.4 47.1 1.0 CHC B:HEM901 3.4 51.3 1.0 CHD B:HEM901 3.4 51.0 1.0 CHB B:HEM901 3.4 46.3 1.0 CA B:CYS194 4.1 47.8 1.0 C2A B:HEM901 4.2 46.0 1.0 C2C B:HEM901 4.2 58.1 1.0 C3D B:HEM901 4.2 49.3 1.0 C3A B:HEM901 4.3 43.7 1.0 C3C B:HEM901 4.3 57.5 1.0 C2D B:HEM901 4.3 49.7 1.0 C2B B:HEM901 4.3 51.5 1.0 C3B B:HEM901 4.3 49.6 1.0 NE1 B:TRP188 4.3 62.7 1.0 C B:CYS194 4.9 49.3 1.0 N B:ILE195 5.0 47.0 1.0

B.R.Crane, R.A.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