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Zinc in PDB 1m9q: Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound

Enzymatic activity of Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound

All present enzymatic activity of Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound:
1.14.13.39;

Protein crystallography data

The structure of Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound, PDB code: 1m9q was solved by R.J.Rosenfeld, E.D.Garcin, K.Panda, G.Andersson, A.Aberg, A.V.Wallace, D.J.Stuehr, J.A.Tainer, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.09 / 2.01
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.508, 90.888, 155.789, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 22.6

Other elements in 1m9q:

The structure of Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound (pdb code 1m9q). 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 Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound, PDB code: 1m9q:

Zinc binding site 1 out of 1 in 1m9q

Go back to Zinc Binding Sites List in 1m9q
Zinc binding site 1 out of 1 in the Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn903

b:30.2
occ:1.00
 SG B:CYS94 2.3 32.5 1.0
SG B:CYS99 2.3 30.7 1.0
SG A:CYS94 2.3 30.8 1.0
SG A:CYS99 2.3 30.9 1.0
CB A:CYS99 3.2 32.2 1.0
CB B:CYS99 3.2 32.0 1.0
CB B:CYS94 3.4 37.4 1.0
CB A:CYS94 3.4 35.1 1.0
CA A:CYS99 3.7 31.9 1.0
CA B:CYS99 3.7 32.2 1.0
N A:GLY101 4.1 34.4 1.0
N B:GLY101 4.2 33.7 1.0
N A:LEU100 4.2 32.8 1.0
N B:LEU100 4.2 32.0 1.0
C A:CYS99 4.3 32.8 1.0
C B:CYS99 4.4 32.1 1.0
CA B:GLY101 4.5 33.0 1.0
CA A:GLY101 4.5 33.2 1.0
O A:HOH1142 4.6 42.9 1.0
CA B:CYS94 4.7 38.0 1.0
CA A:CYS94 4.8 37.8 1.0
O B:HOH1061 4.8 42.4 1.0
N A:CYS99 5.0 33.8 1.0

Reference:

R.J.Rosenfeld, E.D.Garcin, K.Panda, G.Andersson, A.Aberg, A.V.Wallace, G.M.Morris, A.J.Olson, D.J.Stuehr, J.A.Tainer, E.D.Getzoff. Conformational Changes in Nitric Oxide Synthases Induced By Chlorzoxazone and Nitroindazoles: Crystallographic and Computational Analyses of Inhibitor Potency Biochemistry V. 41 13915 2002.
ISSN: ISSN 0006-2960
PubMed: 12437348
DOI: 10.1021/BI026313J
Page generated: Sun Oct 13 05:29:17 2024

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