Iron in PDB 1foi: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1400W(H4B-Free)

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1400W(H4B-Free):
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1400W(H4B-Free), PDB code: 1foi was solved by C.S.Raman, H.Li, P.Martasek, 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)	39.08 / 1.93
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.191, 106.645, 156.300, 90.00, 90.00, 90.00
R / Rfree (%)	22.2 / 25.1

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1400W(H4B-Free) also contains other interesting chemical elements:

Arsenic	(As)	2 atoms
Zinc	(Zn)	1 atom

The binding sites of Iron atom in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1400W(H4B-Free) (pdb code 1foi). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1400W(H4B-Free), PDB code: 1foi:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1400W(H4B-Free)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1400W(H4B-Free) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:25.3 occ:1.00 FE A:HEM500 0.0 25.3 1.0 NB A:HEM500 2.0 25.4 1.0 ND A:HEM500 2.0 26.0 1.0 NC A:HEM500 2.0 25.4 1.0 NA A:HEM500 2.0 26.2 1.0 SG A:CYS186 2.3 25.6 1.0 C1B A:HEM500 3.0 25.5 1.0 C4B A:HEM500 3.0 25.4 1.0 C1D A:HEM500 3.1 26.1 1.0 C4C A:HEM500 3.1 25.4 1.0 C1C A:HEM500 3.1 25.3 1.0 C4A A:HEM500 3.1 26.1 1.0 C1A A:HEM500 3.1 26.6 1.0 C4D A:HEM500 3.1 26.5 1.0 CB A:CYS186 3.3 25.1 1.0 CHB A:HEM500 3.4 25.6 1.0 CHD A:HEM500 3.4 25.6 1.0 CHC A:HEM500 3.5 25.0 1.0 CHA A:HEM500 3.5 26.2 1.0 CA A:CYS186 4.0 25.1 1.0 C7 A:14W810 4.2 37.0 1.0 C2B A:HEM500 4.2 25.3 1.0 C3B A:HEM500 4.3 25.4 1.0 C2D A:HEM500 4.3 26.6 1.0 C2A A:HEM500 4.3 27.0 1.0 C2C A:HEM500 4.3 24.9 1.0 C3D A:HEM500 4.3 27.0 1.0 C3A A:HEM500 4.3 26.6 1.0 C3C A:HEM500 4.3 25.1 1.0 N8 A:14W810 4.3 36.6 1.0 NE1 A:TRP180 4.4 23.2 1.0 C10 A:14W810 4.4 36.4 1.0 C9 A:14W810 4.5 36.5 1.0 N A:GLY188 4.8 25.6 1.0 C A:CYS186 4.8 25.2 1.0 N A:VAL187 4.9 25.1 1.0 CD1 A:TRP180 5.0 23.4 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1400W(H4B-Free)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1400W(H4B-Free) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:25.8 occ:1.00 FE B:HEM500 0.0 25.8 1.0 ND B:HEM500 2.0 26.9 1.0 NB B:HEM500 2.0 26.3 1.0 NC B:HEM500 2.0 26.5 1.0 NA B:HEM500 2.0 26.5 1.0 SG B:CYS186 2.2 26.6 1.0 C1B B:HEM500 3.1 26.0 1.0 C1D B:HEM500 3.1 26.9 1.0 C4D B:HEM500 3.1 27.1 1.0 C1C B:HEM500 3.1 26.3 1.0 C4C B:HEM500 3.1 26.3 1.0 C4B B:HEM500 3.1 26.1 1.0 C4A B:HEM500 3.1 26.2 1.0 C1A B:HEM500 3.1 26.5 1.0 CB B:CYS186 3.3 26.5 1.0 CHC B:HEM500 3.4 26.2 1.0 CHD B:HEM500 3.4 26.5 1.0 CHB B:HEM500 3.5 26.1 1.0 CHA B:HEM500 3.5 26.7 1.0 CA B:CYS186 4.1 26.4 1.0 NE1 B:TRP180 4.2 25.5 1.0 C3D B:HEM500 4.3 27.6 1.0 C2D B:HEM500 4.3 27.1 1.0 C2B B:HEM500 4.3 26.1 1.0 C7 B:14W810 4.3 37.2 1.0 C2C B:HEM500 4.3 26.4 1.0 C3A B:HEM500 4.3 26.5 1.0 C3C B:HEM500 4.3 26.4 1.0 C3B B:HEM500 4.3 26.0 1.0 C2A B:HEM500 4.3 26.7 1.0 C10 B:14W810 4.3 36.8 1.0 N8 B:14W810 4.5 36.8 1.0 C9 B:14W810 4.5 36.9 1.0 C B:CYS186 4.9 26.4 1.0 CD1 B:TRP180 4.9 25.7 1.0 N B:GLY188 5.0 26.9 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