Iron in PDB 1zvl: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg.

All present enzymatic activity of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg.:
1.14.13.39;

The structure of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg., PDB code: 1zvl was solved by H.Matter, H.S.Kumar, R.Fedorov, A.Frey, P.Kotsonis, E.Hartmann, L.G.Frohlich, A.Reif, W.Pfleiderer, P.Scheurer, D.K.Ghosh, I.Schlichting, H.H.Schmidt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.360, 111.289, 165.184, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 24.9

The structure of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg. also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Iron atom in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg. (pdb code 1zvl). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg., PDB code: 1zvl:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:22.4 occ:1.00 FE A:HEM800 0.0 22.4 1.0 ND A:HEM800 1.9 24.9 1.0 NB A:HEM800 2.0 24.5 1.0 NA A:HEM800 2.1 17.9 1.0 NC A:HEM800 2.2 39.3 1.0 SG A:CYS415 2.3 27.3 1.0 C1D A:HEM800 3.0 33.1 1.0 C4D A:HEM800 3.0 25.5 1.0 C4B A:HEM800 3.1 30.4 1.0 C1B A:HEM800 3.1 26.5 1.0 C4A A:HEM800 3.1 18.6 1.0 C1A A:HEM800 3.1 13.9 1.0 C4C A:HEM800 3.2 36.6 1.0 C1C A:HEM800 3.2 32.8 1.0 CB A:CYS415 3.3 17.9 1.0 CHA A:HEM800 3.4 19.2 1.0 CHD A:HEM800 3.4 38.5 1.0 CHB A:HEM800 3.4 22.1 1.0 CHC A:HEM800 3.5 32.7 1.0 NH1 A:ARG901 4.0 23.9 1.0 CA A:CYS415 4.1 24.1 1.0 C2D A:HEM800 4.2 23.8 1.0 C3D A:HEM800 4.2 21.1 1.0 C2B A:HEM800 4.3 21.7 1.0 C3B A:HEM800 4.3 25.2 1.0 C3A A:HEM800 4.3 27.9 1.0 C2A A:HEM800 4.3 19.5 1.0 C2C A:HEM800 4.4 32.5 1.0 NE1 A:TRP409 4.4 20.6 1.0 C3C A:HEM800 4.4 32.4 1.0 CZ A:ARG901 4.5 31.1 1.0 N A:VAL416 4.8 23.8 1.0 NH2 A:ARG901 4.8 26.7 1.0 N A:GLY417 4.8 21.0 1.0 C A:CYS415 4.8 20.8 1.0

Iron binding site 2 out of 2 in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe800 b:22.1 occ:1.00 FE B:HEM800 0.0 22.1 1.0 NB B:HEM800 2.0 23.4 1.0 ND B:HEM800 2.0 16.5 1.0 NA B:HEM800 2.1 14.1 1.0 NC B:HEM800 2.1 26.0 1.0 SG B:CYS415 2.2 24.5 1.0 C1D B:HEM800 3.0 24.6 1.0 C1B B:HEM800 3.0 27.4 1.0 C4B B:HEM800 3.1 21.6 1.0 C4A B:HEM800 3.1 14.5 1.0 C4D B:HEM800 3.1 19.1 1.0 C1A B:HEM800 3.1 17.7 1.0 C4C B:HEM800 3.1 19.0 1.0 C1C B:HEM800 3.2 21.8 1.0 CHD B:HEM800 3.4 22.2 1.0 CHB B:HEM800 3.4 18.2 1.0 CB B:CYS415 3.4 18.5 1.0 CHA B:HEM800 3.5 15.4 1.0 CHC B:HEM800 3.5 20.8 1.0 NH1 B:ARG921 3.9 20.3 1.0 CA B:CYS415 4.2 14.6 1.0 C2B B:HEM800 4.2 22.2 1.0 C2D B:HEM800 4.3 21.5 1.0 C3B B:HEM800 4.3 15.8 1.0 C3D B:HEM800 4.3 16.8 1.0 C3A B:HEM800 4.3 19.3 1.0 C2A B:HEM800 4.3 20.0 1.0 C3C B:HEM800 4.4 23.5 1.0 NE1 B:TRP409 4.4 17.5 1.0 C2C B:HEM800 4.5 19.6 1.0 CZ B:ARG921 4.5 29.2 1.0 N B:GLY417 4.8 28.6 1.0 C B:CYS415 4.9 21.0 1.0 N B:VAL416 4.9 21.6 1.0 NH2 B:ARG921 5.0 18.1 1.0

H.Matter, H.S.Kumar, R.Fedorov, A.Frey, P.Kotsonis, E.Hartmann, L.G.Frohlich, A.Reif, W.Pfleiderer, P.Scheurer, D.K.Ghosh, I.Schlichting, H.H.Schmidt. Structural Analysis of Isoform-Specific Inhibitors Targeting the Tetrahydrobiopterin Binding Site of Human Nitric Oxide Synthases. J.Med.Chem. V. 48 4783 2005.
ISSN: ISSN 0022-2623
PubMed: 16033258
DOI: 10.1021/JM050007X