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Zinc in PDB 1vag: Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477

Enzymatic activity of Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477

All present enzymatic activity of Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477:
1.14.13.39;

Protein crystallography data

The structure of Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477, PDB code: 1vag was solved by R.Fedorov, R.Vasan, D.K.Ghosh, I.Schlichting, 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 (°) 45.269, 109.199, 164.885, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 22.9

Other elements in 1vag:

The structure of Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477 also contains other interesting chemical elements:

Iron (Fe) 1 atom
Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477 (pdb code 1vag). 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 Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477, PDB code: 1vag:

Zinc binding site 1 out of 1 in 1vag

Go back to Zinc Binding Sites List in 1vag
Zinc binding site 1 out of 1 in the Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Neuronal Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn950

b:21.2
occ:0.50
SG A:CYS331 2.3 22.2 1.0
SG A:CYS326 2.4 19.9 1.0
CB A:CYS331 3.3 19.2 1.0
CB A:CYS326 3.5 23.0 1.0
CA A:CYS331 3.6 18.6 1.0
N A:MET332 4.0 14.2 1.0
N A:GLY333 4.1 17.0 1.0
C A:CYS331 4.2 19.9 1.0
CA A:GLY333 4.5 18.2 1.0
CA A:CYS326 4.8 32.2 1.0
C A:MET332 4.9 20.6 1.0
N A:CYS331 4.9 18.9 1.0

Reference:

R.Fedorov, R.Vasan, D.K.Ghosh, I.Schlichting. Structures of Nitric Oxide Synthase Isoforms Complexed with the Inhibitor Ar-R17477 Suggest A Rational Basis For Specificity and Inhibitor Design Proc.Natl.Acad.Sci.Usa V. 101 5892 2004.
ISSN: ISSN 0027-8424
PubMed: 15071192
DOI: 10.1073/PNAS.0306588101
Page generated: Mon Jan 25 16:15:10 2021

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