Zinc 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:

Iron

(Fe)

4 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex, PDB code: 1nsi:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Inducible Nitric Oxide Synthase, Zn-Bound, L-Arg Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn 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:Zn901 b:58.3 occ:1.00 SG B:CYS110 2.3 48.0 1.0 SG A:CYS115 2.3 49.2 1.0 SG B:CYS115 2.3 52.8 1.0 SG A:CYS110 2.3 53.0 1.0 CB B:CYS115 3.3 54.9 1.0 CB A:CYS110 3.3 62.6 1.0 CB B:CYS110 3.4 60.7 1.0 CB A:CYS115 3.5 53.5 1.0 CA B:CYS115 3.8 58.0 1.0 CA A:CYS115 4.0 55.9 1.0 N B:LEU116 4.2 54.0 1.0 N B:GLY117 4.3 50.2 1.0 C B:CYS115 4.4 55.5 1.0 N A:LEU116 4.5 53.8 1.0 N A:GLY117 4.5 51.8 1.0 C A:CYS115 4.6 53.5 1.0 CA B:GLY117 4.7 46.7 1.0 CA B:CYS110 4.7 66.8 1.0 CA A:CYS110 4.7 68.0 1.0 CA A:GLY117 4.8 50.5 1.0

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn 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 C:Zn902 b:63.3 occ:1.00 SG C:CYS115 2.3 62.3 1.0 SG D:CYS115 2.3 56.4 1.0 SG C:CYS110 2.3 66.3 1.0 SG D:CYS110 2.4 67.7 1.0 CB C:CYS115 3.1 69.4 1.0 CB D:CYS115 3.4 57.4 1.0 CB C:CYS110 3.4 78.0 1.0 CB D:CYS110 3.6 76.4 1.0 CA C:CYS115 3.7 69.1 1.0 CA D:CYS115 4.0 62.0 1.0 N C:LEU116 4.2 68.5 1.0 C C:CYS115 4.3 68.2 1.0 N D:LEU116 4.3 58.9 1.0 N D:GLY117 4.4 57.6 1.0 C D:CYS115 4.4 60.7 1.0 N C:GLY117 4.5 62.9 1.0 CA D:GLY117 4.7 53.2 1.0 CA C:CYS110 4.8 78.5 1.0 CA C:GLY117 4.8 58.5 1.0 CA D:CYS110 4.9 79.1 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