Iron in PDB 4nos: Human Inducible Nitric Oxide Synthase with Inhibitor

All present enzymatic activity of Human Inducible Nitric Oxide Synthase with Inhibitor:
1.14.13.39;

The structure of Human Inducible Nitric Oxide Synthase with Inhibitor, PDB code: 4nos was solved by T.O.Fischmann, P.C.Weber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	89.759, 156.672, 190.044, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 28.9

The structure of Human Inducible Nitric Oxide Synthase with Inhibitor also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Human Inducible Nitric Oxide Synthase with Inhibitor (pdb code 4nos). 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 with Inhibitor, PDB code: 4nos:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Human Inducible Nitric Oxide Synthase with Inhibitor


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 with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe510 b:21.8 occ:1.00 FE A:HEM510 0.0 21.8 1.0 NB A:HEM510 2.1 24.0 1.0 ND A:HEM510 2.1 17.4 1.0 NC A:HEM510 2.1 30.4 1.0 NA A:HEM510 2.1 23.2 1.0 SG A:CYS200 2.4 18.5 1.0 C1C A:HEM510 3.1 28.0 1.0 C1B A:HEM510 3.1 23.1 1.0 C4B A:HEM510 3.1 24.3 1.0 C1A A:HEM510 3.1 20.1 1.0 C4D A:HEM510 3.1 17.9 1.0 C4A A:HEM510 3.1 23.7 1.0 C1D A:HEM510 3.1 17.6 1.0 C4C A:HEM510 3.2 28.5 1.0 CHC A:HEM510 3.4 26.3 1.0 CHB A:HEM510 3.5 24.0 1.0 CHA A:HEM510 3.5 19.8 1.0 CHD A:HEM510 3.5 23.3 1.0 CB A:CYS200 3.6 19.5 1.0 C2 A:ITU512 4.1 34.5 1.0 S A:ITU512 4.2 48.8 1.0 CA A:CYS200 4.2 17.0 1.0 C2B A:HEM510 4.3 21.8 1.0 C3B A:HEM510 4.3 23.0 1.0 C2A A:HEM510 4.3 22.0 1.0 C3A A:HEM510 4.3 21.1 1.0 C3D A:HEM510 4.3 16.7 1.0 C1 A:ITU512 4.3 33.2 1.0 C2D A:HEM510 4.3 18.4 1.0 C2C A:HEM510 4.4 28.9 1.0 C3C A:HEM510 4.4 27.4 1.0 NE1 A:TRP194 4.4 19.3 1.0 N A:GLY202 4.6 22.9 1.0 C3 A:ITU512 4.7 47.4 1.0 C A:CYS200 4.8 18.9 1.0 N A:ILE201 4.9 22.0 1.0 CA A:GLY202 4.9 20.8 1.0

Iron binding site 2 out of 4 in the Human Inducible Nitric Oxide Synthase with Inhibitor


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 with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1010 b:20.5 occ:1.00 FE B:HEM1010 0.0 20.5 1.0 ND B:HEM1010 2.0 2.0 1.0 NB B:HEM1010 2.0 4.9 1.0 NA B:HEM1010 2.1 10.1 1.0 NC B:HEM1010 2.1 10.2 1.0 SG B:CYS200 2.4 17.3 1.0 C1B B:HEM1010 3.0 13.0 1.0 C4A B:HEM1010 3.0 9.2 1.0 C1D B:HEM1010 3.1 5.9 1.0 C4D B:HEM1010 3.1 6.0 1.0 C1A B:HEM1010 3.1 8.5 1.0 C4B B:HEM1010 3.1 9.2 1.0 C1C B:HEM1010 3.1 6.7 1.0 C4C B:HEM1010 3.1 8.2 1.0 CHB B:HEM1010 3.3 8.5 1.0 CB B:CYS200 3.4 12.7 1.0 CHD B:HEM1010 3.4 7.2 1.0 CHA B:HEM1010 3.5 5.2 1.0 CHC B:HEM1010 3.5 6.9 1.0 S B:ITU1012 4.0 40.8 1.0 C2 B:ITU1012 4.2 28.1 1.0 CA B:CYS200 4.2 13.4 1.0 C2B B:HEM1010 4.2 11.8 1.0 C3A B:HEM1010 4.3 13.5 1.0 C3B B:HEM1010 4.3 9.4 1.0 C2D B:HEM1010 4.3 5.5 1.0 C3D B:HEM1010 4.3 7.7 1.0 C2A B:HEM1010 4.3 14.6 1.0 C3C B:HEM1010 4.4 9.9 1.0 C2C B:HEM1010 4.4 9.7 1.0 NE1 B:TRP194 4.5 10.0 1.0 C3 B:ITU1012 4.5 41.8 1.0 C1 B:ITU1012 4.5 34.3 1.0 N B:GLY202 4.7 20.0 1.0 N2 B:ITU1012 4.8 39.3 1.0 C B:CYS200 4.9 12.9 1.0 N B:ILE201 4.9 13.4 1.0

Iron binding site 3 out of 4 in the Human Inducible Nitric Oxide Synthase with Inhibitor


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 with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe2010 b:17.9 occ:1.00 FE C:HEM2010 0.0 17.9 1.0 NC C:HEM2010 2.1 22.9 1.0 NA C:HEM2010 2.1 16.2 1.0 ND C:HEM2010 2.1 21.6 1.0 NB C:HEM2010 2.2 26.0 1.0 SG C:CYS200 2.3 16.6 1.0 C1A C:HEM2010 3.1 19.5 1.0 C4C C:HEM2010 3.1 21.1 1.0 C1C C:HEM2010 3.1 24.0 1.0 C4D C:HEM2010 3.1 18.3 1.0 C4A C:HEM2010 3.1 18.6 1.0 C1D C:HEM2010 3.1 18.1 1.0 C1B C:HEM2010 3.1 20.7 1.0 C4B C:HEM2010 3.2 23.5 1.0 CB C:CYS200 3.3 15.2 1.0 CHD C:HEM2010 3.4 22.5 1.0 CHA C:HEM2010 3.4 16.6 1.0 CHB C:HEM2010 3.5 19.1 1.0 CHC C:HEM2010 3.5 22.5 1.0 S C:ITU2012 3.8 43.9 1.0 C2 C:ITU2012 3.9 37.4 1.0 C1 C:ITU2012 4.0 43.1 1.0 CA C:CYS200 4.1 13.3 1.0 C2A C:HEM2010 4.3 19.4 1.0 C3A C:HEM2010 4.3 20.1 1.0 C3C C:HEM2010 4.3 21.9 1.0 C2C C:HEM2010 4.3 22.3 1.0 C3D C:HEM2010 4.3 17.4 1.0 C2D C:HEM2010 4.3 17.2 1.0 C2B C:HEM2010 4.4 22.9 1.0 C3B C:HEM2010 4.4 21.6 1.0 NE1 C:TRP194 4.4 20.0 1.0 C3 C:ITU2012 4.6 45.2 1.0 N C:GLY202 4.7 17.2 1.0 C C:CYS200 4.8 10.4 1.0 N C:ILE201 4.9 12.8 1.0 N2 C:ITU2012 5.0 45.0 1.0

Iron binding site 4 out of 4 in the Human Inducible Nitric Oxide Synthase with Inhibitor


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 with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe3010 b:17.8 occ:1.00 FE D:HEM3010 0.0 17.8 1.0 ND D:HEM3010 2.0 2.0 1.0 NC D:HEM3010 2.1 17.9 1.0 NB D:HEM3010 2.1 10.9 1.0 NA D:HEM3010 2.1 14.6 1.0 SG D:CYS200 2.5 17.2 1.0 C1D D:HEM3010 3.0 10.8 1.0 C4D D:HEM3010 3.0 9.7 1.0 C4C D:HEM3010 3.1 16.0 1.0 C1A D:HEM3010 3.1 13.8 1.0 C1C D:HEM3010 3.1 16.8 1.0 C1B D:HEM3010 3.1 16.1 1.0 C4B D:HEM3010 3.1 15.3 1.0 C4A D:HEM3010 3.2 10.8 1.0 CHD D:HEM3010 3.4 13.6 1.0 CHA D:HEM3010 3.4 9.7 1.0 CHC D:HEM3010 3.5 16.2 1.0 CB D:CYS200 3.5 16.4 1.0 CHB D:HEM3010 3.5 15.1 1.0 S D:ITU3012 3.8 38.5 1.0 C2D D:HEM3010 4.2 7.0 1.0 C2 D:ITU3012 4.2 35.8 1.0 C3D D:HEM3010 4.2 7.7 1.0 CA D:CYS200 4.3 13.6 1.0 C2A D:HEM3010 4.3 18.1 1.0 C3C D:HEM3010 4.3 18.6 1.0 C2B D:HEM3010 4.3 15.7 1.0 C3B D:HEM3010 4.4 10.1 1.0 C2C D:HEM3010 4.4 19.9 1.0 C3A D:HEM3010 4.4 16.8 1.0 NE1 D:TRP194 4.4 14.0 1.0 C1 D:ITU3012 4.4 43.9 1.0 C3 D:ITU3012 4.5 44.0 1.0 N D:GLY202 4.7 15.7 1.0 N D:ILE201 4.9 14.1 1.0 N1 D:ITU3012 4.9 39.8 1.0 C D:CYS200 4.9 12.5 1.0

T.O.Fischmann, A.Hruza, X.D.Niu, J.D.Fossetta, C.A.Lunn, E.Dolphin, A.J.Prongay, P.Reichert, D.J.Lundell, S.K.Narula, P.C.Weber. Structural Characterization of Nitric Oxide Synthase Isoforms Reveals Striking Active-Site Conservation. Nat.Struct.Biol. V. 6 233 1999.
ISSN: ISSN 1072-8368
PubMed: 10074942
DOI: 10.1038/6675