Zinc in PDB 1zvi: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain

All present enzymatic activity of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain:
1.14.13.39;

The structure of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain, PDB code: 1zvi 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 / 2.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	43.183, 107.522, 163.027, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 25.5

The structure of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Zinc atom in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain (pdb code 1zvi). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain, PDB code: 1zvi:

Zinc binding site 1 out of 1 in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn902 b:31.5 occ:0.50 SG A:CYS331 2.5 33.6 1.0 SG A:CYS326 2.5 35.5 1.0 CB A:CYS331 3.4 20.4 1.0 CB A:CYS326 3.6 19.4 1.0 CA A:CYS331 3.7 29.4 1.0 N A:MET332 4.1 32.1 1.0 N A:GLY333 4.2 27.8 1.0 C A:CYS331 4.3 33.9 1.0 CA A:GLY333 4.5 27.0 1.0 O A:ILE330 4.7 23.9 1.0 N A:CYS331 4.9 28.4 1.0 CA A:CYS326 4.9 35.2 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