Iron in PDB 1nsi: Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex

All present enzymatic activity of Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex:
1.14.13.39;

The structure of Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex, PDB code: 1nsi was solved by H.Li, C.S.Raman, C.B.Glaser, E.Blasko, T.A.Young, J.F.Parkinson, M.Whitlow, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.55
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	187.350, 187.350, 227.490, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 24.3

The structure of Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex (pdb code 1nsi). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex, PDB code: 1nsi:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe550 b:23.5 occ:1.00 FE A:HEM550 0.0 23.5 1.0 NC A:HEM550 1.9 38.8 1.0 NB A:HEM550 1.9 34.2 1.0 NA A:HEM550 2.0 36.0 1.0 ND A:HEM550 2.0 41.0 1.0 SG A:CYS200 2.2 20.9 1.0 C1C A:HEM550 2.9 37.2 1.0 C4C A:HEM550 3.0 38.4 1.0 C4B A:HEM550 3.0 32.0 1.0 C1B A:HEM550 3.0 33.3 1.0 C4A A:HEM550 3.0 34.0 1.0 C1A A:HEM550 3.0 34.5 1.0 C1D A:HEM550 3.1 38.9 1.0 C4D A:HEM550 3.1 38.1 1.0 CHC A:HEM550 3.3 35.5 1.0 CHB A:HEM550 3.4 29.5 1.0 CHD A:HEM550 3.4 34.3 1.0 CHA A:HEM550 3.4 35.9 1.0 CB A:CYS200 3.4 38.9 1.0 CA A:CYS200 4.1 39.0 1.0 C2C A:HEM550 4.2 35.8 1.0 C3C A:HEM550 4.2 37.0 1.0 C3B A:HEM550 4.2 29.5 1.0 C2B A:HEM550 4.2 28.7 1.0 C3A A:HEM550 4.3 35.9 1.0 C2A A:HEM550 4.3 33.6 1.0 C3D A:HEM550 4.3 35.3 1.0 C2D A:HEM550 4.3 35.1 1.0 NH1 A:ARG700 4.4 45.6 1.0 CZ A:ARG700 4.5 46.5 1.0 NE1 A:TRP194 4.5 30.8 1.0 NH2 A:ARG700 4.7 44.3 1.0 N A:ILE201 4.8 37.2 1.0 N A:GLY202 4.8 33.8 1.0 C A:CYS200 4.9 37.1 1.0 NE A:ARG700 5.0 45.7 1.0

Iron binding site 2 out of 4 in the Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe550 b:46.0 occ:1.00 FE B:HEM550 0.0 46.0 1.0 ND B:HEM550 1.9 39.9 1.0 NC B:HEM550 1.9 45.2 1.0 NB B:HEM550 2.0 36.7 1.0 NA B:HEM550 2.0 37.0 1.0 SG B:CYS200 2.2 40.8 1.0 C1D B:HEM550 2.9 44.0 1.0 C4D B:HEM550 3.0 41.6 1.0 C1C B:HEM550 3.0 49.4 1.0 C4B B:HEM550 3.0 38.5 1.0 C4C B:HEM550 3.0 45.9 1.0 C1B B:HEM550 3.0 36.0 1.0 C1A B:HEM550 3.0 36.9 1.0 C4A B:HEM550 3.1 34.4 1.0 CB B:CYS200 3.1 30.8 1.0 CHC B:HEM550 3.3 44.4 1.0 CHD B:HEM550 3.3 44.9 1.0 CHA B:HEM550 3.4 41.8 1.0 CHB B:HEM550 3.4 33.3 1.0 CA B:CYS200 3.7 39.8 1.0 C2D B:HEM550 4.2 40.7 1.0 C3D B:HEM550 4.2 39.4 1.0 C2C B:HEM550 4.2 44.7 1.0 C3B B:HEM550 4.2 37.4 1.0 C3C B:HEM550 4.2 44.1 1.0 C2B B:HEM550 4.3 34.6 1.0 C3A B:HEM550 4.3 34.9 1.0 C2A B:HEM550 4.3 32.7 1.0 NE1 B:TRP194 4.5 40.1 1.0 NH1 B:ARG701 4.5 56.6 1.0 C B:CYS200 4.6 38.4 1.0 CZ B:ARG701 4.7 54.0 1.0 N B:ILE201 4.7 34.3 1.0 N B:GLY202 4.8 34.6 1.0 N B:CYS200 4.9 40.0 1.0

Iron binding site 3 out of 4 in the Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe550 b:28.5 occ:1.00 FE C:HEM550 0.0 28.5 1.0 NC C:HEM550 1.9 38.0 1.0 ND C:HEM550 1.9 39.8 1.0 NA C:HEM550 1.9 30.5 1.0 NB C:HEM550 2.0 38.7 1.0 SG C:CYS200 2.2 18.5 1.0 C1A C:HEM550 2.9 31.8 1.0 C4D C:HEM550 2.9 34.1 1.0 C1C C:HEM550 3.0 38.6 1.0 C4C C:HEM550 3.0 36.9 1.0 C1D C:HEM550 3.0 36.1 1.0 C4A C:HEM550 3.0 29.5 1.0 C4B C:HEM550 3.0 37.5 1.0 C1B C:HEM550 3.0 35.6 1.0 CHA C:HEM550 3.3 29.1 1.0 CHC C:HEM550 3.3 38.9 1.0 CHD C:HEM550 3.4 36.6 1.0 CB C:CYS200 3.4 33.6 1.0 CHB C:HEM550 3.4 26.9 1.0 CA C:CYS200 4.1 35.2 1.0 NH1 C:ARG702 4.1 43.2 1.0 C3D C:HEM550 4.2 31.6 1.0 C2A C:HEM550 4.2 30.3 1.0 C3A C:HEM550 4.2 30.0 1.0 C2D C:HEM550 4.2 31.7 1.0 C2C C:HEM550 4.2 36.4 1.0 C3C C:HEM550 4.2 36.5 1.0 C2B C:HEM550 4.2 34.2 1.0 C3B C:HEM550 4.3 33.4 1.0 NE1 C:TRP194 4.3 39.5 1.0 CZ C:ARG702 4.4 42.0 1.0 NH2 C:ARG702 4.7 38.8 1.0 N C:GLY202 4.8 28.6 1.0 C C:CYS200 4.8 32.6 1.0 N C:ILE201 5.0 29.6 1.0 NE C:ARG702 5.0 40.0 1.0

Iron binding site 4 out of 4 in the Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe550 b:58.3 occ:1.00 FE D:HEM550 0.0 58.3 1.0 NC D:HEM550 1.9 55.6 1.0 ND D:HEM550 1.9 50.3 1.0 NA D:HEM550 1.9 52.7 1.0 NB D:HEM550 2.0 51.5 1.0 SG D:CYS200 2.2 55.9 1.0 C1C D:HEM550 3.0 54.7 1.0 C4C D:HEM550 3.0 57.0 1.0 C4A D:HEM550 3.0 51.5 1.0 C4D D:HEM550 3.0 54.4 1.0 C1D D:HEM550 3.0 53.2 1.0 C1A D:HEM550 3.0 52.5 1.0 C1B D:HEM550 3.0 53.0 1.0 C4B D:HEM550 3.0 50.6 1.0 CHC D:HEM550 3.4 49.3 1.0 CHD D:HEM550 3.4 55.3 1.0 CHB D:HEM550 3.4 52.8 1.0 CHA D:HEM550 3.4 55.1 1.0 CB D:CYS200 3.5 47.0 1.0 CA D:CYS200 4.2 51.5 1.0 C2C D:HEM550 4.2 55.0 1.0 C3C D:HEM550 4.2 57.0 1.0 C3A D:HEM550 4.2 51.0 1.0 C3D D:HEM550 4.2 50.5 1.0 C3B D:HEM550 4.2 52.4 1.0 C2D D:HEM550 4.2 50.4 1.0 C2A D:HEM550 4.2 50.8 1.0 C2B D:HEM550 4.2 51.5 1.0 NH1 D:ARG703 4.3 66.9 1.0 CZ D:ARG703 4.5 67.7 1.0 NE1 D:TRP194 4.6 66.1 1.0 NH2 D:ARG703 4.8 64.0 1.0 NE D:ARG703 4.9 70.1 1.0 N D:ILE201 4.9 54.0 1.0 C D:CYS200 5.0 52.3 1.0 N D:GLY202 5.0 56.0 1.0

H.Li, C.S.Raman, C.B.Glaser, E.Blasko, T.A.Young, J.F.Parkinson, M.Whitlow, T.L.Poulos. Crystal Structures of Zinc-Free and -Bound Heme Domain of Human Inducible Nitric-Oxide Synthase. Implications For Dimer Stability and Comparison with Endothelial Nitric-Oxide Synthase. J.Biol.Chem. V. 274 21276 1999.
ISSN: ISSN 0021-9258
PubMed: 10409685
DOI: 10.1074/JBC.274.30.21276