Zinc in PDB 1mmw: Rat Neuronal Nos Heme Domain with Vinyl-L-Nio Bound

All present enzymatic activity of Rat Neuronal Nos Heme Domain with Vinyl-L-Nio Bound:
1.14.13.39;

The structure of Rat Neuronal Nos Heme Domain with Vinyl-L-Nio Bound, PDB code: 1mmw was solved by L.E.Bretscher, H.Li, T.L.Poulos, O.W.Griffith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.25 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.690, 109.980, 164.540, 90.00, 90.00, 90.00
R / Rfree (%)	23.1 / 26.6

The structure of Rat Neuronal Nos Heme Domain with Vinyl-L-Nio Bound also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Zinc atom in the Rat Neuronal Nos Heme Domain with Vinyl-L-Nio Bound (pdb code 1mmw). 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 Nos Heme Domain with Vinyl-L-Nio Bound, PDB code: 1mmw:

Zinc binding site 1 out of 1 in the Rat Neuronal Nos Heme Domain with Vinyl-L-Nio Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Rat Neuronal Nos Heme Domain with Vinyl-L-Nio Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn900 b:55.9 occ:1.00 SG A:CYS331 2.3 58.0 1.0 SG A:CYS326 2.3 60.6 1.0 SG B:CYS326 2.3 58.8 1.0 SG B:CYS331 2.3 58.1 1.0 CB A:CYS331 3.1 59.3 1.0 CB B:CYS331 3.2 58.3 1.0 CB A:CYS326 3.4 63.7 1.0 CB B:CYS326 3.5 61.8 1.0 CA A:CYS331 3.5 59.7 1.0 CA B:CYS331 3.5 58.4 1.0 N A:MET332 3.9 59.3 1.0 N B:MET332 4.0 57.9 1.0 C A:CYS331 4.1 59.5 1.0 C B:CYS331 4.2 58.1 1.0 N A:GLY333 4.2 59.0 1.0 N B:GLY333 4.2 56.9 1.0 CA A:GLY333 4.6 59.0 1.0 CA B:GLY333 4.6 56.7 1.0 CA A:CYS326 4.8 64.6 1.0 N A:CYS331 4.8 60.4 1.0 N B:CYS331 4.8 59.1 1.0 CA B:CYS326 4.9 62.5 1.0 C A:MET332 4.9 59.2 1.0

L.E.Bretscher, H.Li, T.L.Poulos, O.W.Griffith. Structural Characterization and Kinetics of Nitric-Oxide Synthase Inhibition By Novel N5-(Iminoalkyl)- and N5-(Iminoalkenyl)-Ornithines J.Biol.Chem. V. 278 46789 2003.
ISSN: ISSN 0021-9258
PubMed: 12960153
DOI: 10.1074/JBC.M306787200