Zinc in PDB 1nse: Bovine Endothelial Nitric Oxide Synthase

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase:
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase, PDB code: 1nse was solved by C.S.Raman, H.Li, P.Martasek, V.Kral, B.S.S.Masters, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.000, 106.550, 156.220, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 27.8

The binding sites of Zinc atom in the Bovine Endothelial Nitric Oxide Synthase (pdb code 1nse). 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 Bovine Endothelial Nitric Oxide Synthase, PDB code: 1nse:

Zinc binding site 1 out of 1 in the Bovine Endothelial Nitric Oxide Synthase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Bovine Endothelial Nitric Oxide Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn900 b:22.0 occ:1.00 SG A:CYS96 2.3 19.8 1.0 SG A:CYS101 2.4 21.9 1.0 SG B:CYS96 2.4 23.8 1.0 SG B:CYS101 2.4 20.6 1.0 CB B:CYS101 3.1 21.9 1.0 CB A:CYS101 3.2 18.0 1.0 CB A:CYS96 3.3 30.6 1.0 CB B:CYS96 3.5 22.1 1.0 CA B:CYS101 3.7 24.0 1.0 CA A:CYS101 3.7 20.6 1.0 N B:GLY103 4.0 22.7 1.0 N A:GLY103 4.1 24.3 1.0 N A:LEU102 4.1 24.5 1.0 N B:LEU102 4.1 18.6 1.0 C B:CYS101 4.3 27.0 1.0 C A:CYS101 4.3 28.6 1.0 CA A:GLY103 4.4 24.2 1.0 CA B:GLY103 4.4 20.6 1.0 CA A:CYS96 4.7 31.3 1.0 CA B:CYS96 4.8 25.6 1.0 N B:CYS101 4.9 24.2 1.0 N A:CYS101 4.9 20.2 1.0 C A:LEU102 5.0 26.6 1.0 O A:HOH1047 5.0 31.4 1.0 C B:LEU102 5.0 22.6 1.0

C.S.Raman, H.Li, P.Martasek, V.Kral, B.S.Masters, T.L.Poulos. Crystal Structure of Constitutive Endothelial Nitric Oxide Synthase: A Paradigm For Pterin Function Involving A Novel Metal Center. Cell(Cambridge,Mass.) V. 95 939 1998.
ISSN: ISSN 0092-8674
PubMed: 9875848
DOI: 10.1016/S0092-8674(00)81718-3