Iron in PDB 9nse: Bovine Endothelial Nitric Oxide Synthase, Ethyl-Isoselenourea Complex

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase, Ethyl-Isoselenourea Complex:
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase, Ethyl-Isoselenourea Complex, PDB code: 9nse was solved by H.Li, C.S.Raman, 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 / 2.24
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.740, 106.360, 156.300, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 25.4

The structure of Bovine Endothelial Nitric Oxide Synthase, Ethyl-Isoselenourea Complex 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, Ethyl-Isoselenourea Complex (pdb code 9nse). 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, Ethyl-Isoselenourea Complex, PDB code: 9nse:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Bovine Endothelial Nitric Oxide Synthase, Ethyl-Isoselenourea Complex


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, Ethyl-Isoselenourea Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:14.5 occ:1.00 FE A:HEM500 0.0 14.5 1.0 NB A:HEM500 1.9 4.1 1.0 ND A:HEM500 2.0 5.9 1.0 NA A:HEM500 2.0 12.8 1.0 NC A:HEM500 2.0 15.2 1.0 SG A:CYS186 2.2 12.0 1.0 C4B A:HEM500 3.0 16.6 1.0 C1B A:HEM500 3.0 12.2 1.0 C4D A:HEM500 3.0 13.6 1.0 C1A A:HEM500 3.0 13.6 1.0 C1D A:HEM500 3.0 17.9 1.0 C4A A:HEM500 3.1 15.1 1.0 C1C A:HEM500 3.1 8.9 1.0 C4C A:HEM500 3.1 8.8 1.0 CB A:CYS186 3.3 14.2 1.0 CHC A:HEM500 3.4 15.7 1.0 CHA A:HEM500 3.4 6.0 1.0 CHB A:HEM500 3.4 13.3 1.0 CHD A:HEM500 3.5 13.9 1.0 C2 A:ISU800 4.0 8.8 1.0 CA A:CYS186 4.0 10.3 1.0 SE A:ISU800 4.1 27.1 1.0 C2B A:HEM500 4.2 12.3 1.0 C3B A:HEM500 4.2 16.1 1.0 C3D A:HEM500 4.3 13.0 1.0 C2D A:HEM500 4.3 15.0 1.0 C2A A:HEM500 4.3 12.7 1.0 C3A A:HEM500 4.3 13.8 1.0 C2C A:HEM500 4.3 10.0 1.0 NE1 A:TRP180 4.4 9.9 1.0 C3C A:HEM500 4.4 9.6 1.0 C3 A:ISU800 4.6 20.6 1.0 N A:GLY188 4.7 10.0 1.0 C A:CYS186 4.8 10.2 1.0 N A:VAL187 4.8 10.6 1.0 N1 A:ISU800 4.8 13.6 1.0 O A:HOH989 4.9 31.7 1.0 CD1 A:TRP180 5.0 6.7 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase, Ethyl-Isoselenourea Complex


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, Ethyl-Isoselenourea Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:17.5 occ:1.00 FE B:HEM500 0.0 17.5 1.0 ND B:HEM500 2.0 22.9 1.0 NA B:HEM500 2.0 26.3 1.0 NC B:HEM500 2.0 22.7 1.0 NB B:HEM500 2.0 23.3 1.0 SG B:CYS186 2.3 10.8 1.0 C4D B:HEM500 3.0 23.0 1.0 C1D B:HEM500 3.1 26.6 1.0 C1A B:HEM500 3.1 22.1 1.0 C1C B:HEM500 3.1 21.5 1.0 C4B B:HEM500 3.1 25.6 1.0 C4C B:HEM500 3.1 18.9 1.0 C4A B:HEM500 3.1 21.9 1.0 C1B B:HEM500 3.1 21.0 1.0 CB B:CYS186 3.4 19.4 1.0 CHC B:HEM500 3.4 18.6 1.0 CHA B:HEM500 3.4 21.8 1.0 CHD B:HEM500 3.5 20.8 1.0 CHB B:HEM500 3.5 21.3 1.0 SE B:ISU801 4.0 33.3 1.0 C2 B:ISU801 4.0 13.6 1.0 CA B:CYS186 4.1 17.0 1.0 NE1 B:TRP180 4.3 14.1 1.0 C3D B:HEM500 4.3 22.2 1.0 C2D B:HEM500 4.3 20.6 1.0 C2A B:HEM500 4.3 26.8 1.0 C2C B:HEM500 4.3 20.6 1.0 C3B B:HEM500 4.3 21.2 1.0 C3A B:HEM500 4.4 19.6 1.0 C2B B:HEM500 4.4 18.6 1.0 C3C B:HEM500 4.4 21.9 1.0 C3 B:ISU801 4.5 27.9 1.0 N B:GLY188 4.7 18.0 1.0 N1 B:ISU801 4.7 18.5 1.0 N B:VAL187 4.8 19.4 1.0 C B:CYS186 4.8 12.1 1.0 CD1 B:TRP180 4.9 20.1 1.0 O B:HOH1059 4.9 32.6 1.0

H.Li, C.S.Raman, P.Martasek, V.Kral, B.S.Masters, T.L.Poulos. Mapping the Active Site Polarity in Structures of Endothelial Nitric Oxide Synthase Heme Domain Complexed with Isothioureas. J.Inorg.Biochem. V. 81 133 2000.
ISSN: ISSN 0162-0134
PubMed: 11051558
DOI: 10.1016/S0162-0134(00)00099-4