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Zinc in PDB 1fol: Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free)

Enzymatic activity of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free)

All present enzymatic activity of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free):
1.14.13.39;

Protein crystallography data

The structure of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free), PDB code: 1fol was solved by C.S.Raman, H.Li, P.Martasek, B.S.Masters, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.70 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.233, 106.282, 156.291, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 26.5

Other elements in 1fol:

The structure of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free) also contains other interesting chemical elements:

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

Zinc Binding Sites:

The binding sites of Zinc atom in the Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free) (pdb code 1fol). 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 Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free), PDB code: 1fol:

Zinc binding site 1 out of 1 in 1fol

Go back to Zinc Binding Sites List in 1fol
Zinc binding site 1 out of 1 in the Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn900

b:45.7
occ:1.00
 SG B:CYS96 2.3 46.7 1.0
SG A:CYS101 2.3 47.5 1.0
SG B:CYS101 2.3 46.8 1.0
SG A:CYS96 2.3 48.5 1.0
CB B:CYS101 3.2 46.6 1.0
CB A:CYS101 3.2 50.3 1.0
CB B:CYS96 3.5 49.1 1.0
CB A:CYS96 3.6 50.8 1.0
CA B:CYS101 3.7 46.6 1.0
CA A:CYS101 3.7 51.1 1.0
N B:GLY103 4.0 46.3 1.0
N A:GLY103 4.1 50.6 1.0
N B:LEU102 4.1 46.4 1.0
N A:LEU102 4.2 50.4 1.0
C B:CYS101 4.3 46.4 1.0
CA B:GLY103 4.3 46.5 1.0
C A:CYS101 4.3 50.7 1.0
CA A:GLY103 4.5 51.0 1.0
CA B:CYS96 4.8 49.7 1.0
O B:HOH3053 4.8 43.9 1.0
C B:LEU102 5.0 46.1 1.0
N B:CYS101 5.0 47.2 1.0

Reference:

H.Li, C.S.Raman, P.Martasek, B.S.Masters, T.L.Poulos. Crystallographic Studies on Endothelial Nitric Oxide Synthase Complexed with Nitric Oxide and Mechanism-Based Inhibitors Biochemistry V. 40 5399 2001.
ISSN: ISSN 0006-2960
PubMed: 11331003
DOI: 10.1021/BI002658V
Page generated: Sun Oct 13 01:03:34 2024

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