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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1zvl:

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

Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with Natural Substrate L-Arg., PDB code: 1zvl:

Zinc binding site 1 out of 1 in 1zvl

Go back to Zinc Binding Sites List in 1zvl
Zinc binding site 1 out of 1 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 Zinc with other atoms in the Zn 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:Zn950

b:29.4
occ:1.00
 SG A:CYS326 2.1 29.9 1.0
SG B:CYS331 2.2 30.9 1.0
SG A:CYS331 2.3 37.5 1.0
SG B:CYS326 2.5 35.6 1.0
CB B:CYS331 3.1 28.8 1.0
CB A:CYS326 3.3 30.5 1.0
CB A:CYS331 3.3 24.3 1.0
CB B:CYS326 3.5 38.1 1.0
CA B:CYS331 3.6 26.8 1.0
CA A:CYS331 3.7 27.5 1.0
N A:GLY333 4.0 20.6 1.0
N A:MET332 4.2 28.6 1.0
N B:MET332 4.2 32.9 1.0
N B:GLY333 4.3 23.7 1.0
C A:CYS331 4.3 28.2 1.0
C B:CYS331 4.3 29.6 1.0
CA A:GLY333 4.4 15.6 1.0
CA B:GLY333 4.6 25.7 1.0
CA A:CYS326 4.7 40.1 1.0
N B:CYS331 4.8 26.8 1.0
CA B:CYS326 4.9 36.7 1.0
O B:ILE330 4.9 39.4 1.0
O A:ILE330 5.0 28.8 1.0

Reference:

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
Page generated: Wed Oct 16 21:23:10 2024

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