Iron in PDB 1fol: 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;

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

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
Zinc	(Zn)	1 atom

The binding sites of Iron 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 Iron atom.
In total 2 binding sites of Iron where determined in the Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free), PDB code: 1fol:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 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 Iron with other atoms in the Fe 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 A:Fe500 b:34.2 occ:1.00 FE A:HEM500 0.0 34.2 1.0 NA A:HEM500 2.0 34.5 1.0 ND A:HEM500 2.0 34.9 1.0 NC A:HEM500 2.0 34.0 1.0 NB A:HEM500 2.0 33.4 1.0 SG A:CYS186 2.3 35.5 1.0 C1A A:HEM500 3.0 35.2 1.0 C4C A:HEM500 3.0 34.6 1.0 C4A A:HEM500 3.0 34.8 1.0 C1B A:HEM500 3.0 32.8 1.0 C4D A:HEM500 3.0 35.3 1.0 C1D A:HEM500 3.0 34.7 1.0 C1C A:HEM500 3.1 34.2 1.0 C4B A:HEM500 3.1 33.6 1.0 CB A:CYS186 3.4 35.2 1.0 CHD A:HEM500 3.4 34.8 1.0 CHB A:HEM500 3.4 33.9 1.0 CHA A:HEM500 3.4 34.9 1.0 CHC A:HEM500 3.5 33.8 1.0 NH1 A:ARG1700 3.9 39.6 1.0 CA A:CYS186 4.0 35.1 1.0 C3D A:HEM500 4.3 35.5 1.0 C2A A:HEM500 4.3 35.4 1.0 C3A A:HEM500 4.3 35.0 1.0 C3C A:HEM500 4.3 34.3 1.0 C2D A:HEM500 4.3 35.2 1.0 C2B A:HEM500 4.3 32.9 1.0 C2C A:HEM500 4.3 34.1 1.0 C3B A:HEM500 4.3 33.4 1.0 CZ A:ARG1700 4.4 39.7 1.0 NE1 A:TRP180 4.4 32.7 1.0 CD A:ARG1700 4.8 39.9 1.0 NE A:ARG1700 4.8 39.6 1.0 C A:CYS186 4.9 35.2 1.0

Iron binding site 2 out of 2 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 Iron with other atoms in the Fe binding site number 2 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:Fe500 b:34.8 occ:1.00 FE B:HEM500 0.0 34.8 1.0 NB B:HEM500 1.9 33.6 1.0 ND B:HEM500 2.0 34.1 1.0 NA B:HEM500 2.0 34.6 1.0 NC B:HEM500 2.0 33.1 1.0 SG B:CYS186 2.2 34.5 1.0 C1B B:HEM500 3.0 33.8 1.0 C4B B:HEM500 3.0 33.8 1.0 C1D B:HEM500 3.0 34.0 1.0 C4D B:HEM500 3.0 35.0 1.0 C4C B:HEM500 3.0 33.1 1.0 C4A B:HEM500 3.0 34.8 1.0 C1C B:HEM500 3.0 33.5 1.0 C1A B:HEM500 3.1 35.1 1.0 CHB B:HEM500 3.4 34.2 1.0 CHC B:HEM500 3.4 33.5 1.0 CHD B:HEM500 3.4 33.5 1.0 NH1 B:ARG2700 3.5 37.5 1.0 CB B:CYS186 3.5 34.9 1.0 CHA B:HEM500 3.5 34.9 1.0 CZ B:ARG2700 4.1 37.5 1.0 CA B:CYS186 4.1 34.8 1.0 C2B B:HEM500 4.2 33.1 1.0 C2D B:HEM500 4.3 34.6 1.0 C3D B:HEM500 4.3 35.1 1.0 C3B B:HEM500 4.3 33.1 1.0 C3C B:HEM500 4.3 33.3 1.0 C2C B:HEM500 4.3 33.5 1.0 C2A B:HEM500 4.3 35.1 1.0 C3A B:HEM500 4.3 34.9 1.0 NE1 B:TRP180 4.4 33.0 1.0 NH2 B:ARG2700 4.5 37.5 1.0 NE B:ARG2700 4.7 37.0 1.0 C B:CYS186 4.9 34.8 1.0 N B:GLY188 4.9 34.6 1.0 N B:VAL187 4.9 34.5 1.0 CD B:ARG2700 4.9 36.1 1.0

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