Zinc in PDB 3nse: Bovine Enos, H4B-Free, Seitu Complex

All present enzymatic activity of Bovine Enos, H4B-Free, Seitu Complex:
1.14.13.39;

The structure of Bovine Enos, H4B-Free, Seitu Complex, PDB code: 3nse 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)	30.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.170, 107.140, 156.530, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 25.2

The structure of Bovine Enos, H4B-Free, Seitu Complex also contains other interesting chemical elements:

Arsenic	(As)	2 atoms
Iron	(Fe)	2 atoms

The binding sites of Zinc atom in the Bovine Enos, H4B-Free, Seitu Complex (pdb code 3nse). 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 Enos, H4B-Free, Seitu Complex, PDB code: 3nse:

Zinc binding site 1 out of 1 in the Bovine Enos, H4B-Free, Seitu Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Bovine Enos, H4B-Free, Seitu Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn900 b:41.6 occ:1.00 SG B:CYS101 2.3 27.5 1.0 SG A:CYS101 2.3 25.1 1.0 SG A:CYS96 2.3 25.6 1.0 SG B:CYS96 2.3 25.6 1.0 CB B:CYS101 3.1 27.4 1.0 CB A:CYS101 3.2 27.2 1.0 CB B:CYS96 3.4 22.8 1.0 CB A:CYS96 3.6 21.0 1.0 CA B:CYS101 3.6 25.9 1.0 CA A:CYS101 3.7 26.8 1.0 N B:GLY103 4.0 26.0 1.0 N B:LEU102 4.1 22.7 1.0 C B:CYS101 4.2 24.9 1.0 N A:GLY103 4.3 29.4 1.0 CA B:GLY103 4.4 24.0 1.0 N A:LEU102 4.4 27.1 1.0 C A:CYS101 4.4 25.8 1.0 CA A:GLY103 4.5 28.9 1.0 CA B:CYS96 4.8 29.1 1.0 N B:CYS101 4.9 26.6 1.0 C B:LEU102 4.9 24.7 1.0 N A:CYS101 4.9 26.6 1.0 CA A:CYS96 5.0 24.6 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