Iron in PDB 1d0c: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (H4B Free)

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (H4B Free):
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (H4B Free), PDB code: 1d0c was solved by C.S.Raman, H.Li, P.Martasek, G.J.Southan, 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)	8.00 / 1.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.440, 105.980, 155.790, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 25.9

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (H4B Free) also contains other interesting chemical elements:

Bromine	(Br)	4 atoms
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 3- Bromo-7-Nitroindazole (H4B Free) (pdb code 1d0c). 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 3- Bromo-7-Nitroindazole (H4B Free), PDB code: 1d0c:
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 3- Bromo-7-Nitroindazole (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 3- Bromo-7-Nitroindazole (H4B Free) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:18.4 occ:1.00 FE A:HEM500 0.0 18.4 1.0 ND A:HEM500 2.0 16.1 1.0 NB A:HEM500 2.0 18.7 1.0 NA A:HEM500 2.0 21.4 1.0 NC A:HEM500 2.0 18.6 1.0 SG A:CYS186 2.4 19.5 1.0 C4D A:HEM500 3.0 20.4 1.0 C1C A:HEM500 3.0 22.0 1.0 C4A A:HEM500 3.0 18.4 1.0 C4B A:HEM500 3.0 19.2 1.0 C1A A:HEM500 3.0 20.1 1.0 C1D A:HEM500 3.1 18.7 1.0 C4C A:HEM500 3.1 16.2 1.0 C1B A:HEM500 3.1 20.5 1.0 CB A:CYS186 3.4 18.1 1.0 CHC A:HEM500 3.4 18.1 1.0 CHA A:HEM500 3.4 19.7 1.0 CHB A:HEM500 3.5 17.8 1.0 CHD A:HEM500 3.5 17.8 1.0 C9 A:INE760 4.0 21.8 1.0 CA A:CYS186 4.1 18.2 1.0 C4 A:INE760 4.1 23.6 1.0 C3 A:INE760 4.2 18.6 1.0 C3D A:HEM500 4.3 19.4 1.0 C2C A:HEM500 4.3 16.6 1.0 C2A A:HEM500 4.3 17.4 1.0 C2D A:HEM500 4.3 18.4 1.0 C3B A:HEM500 4.3 20.4 1.0 C8 A:INE760 4.3 21.8 1.0 C3A A:HEM500 4.3 18.6 1.0 C2B A:HEM500 4.3 18.1 1.0 C3C A:HEM500 4.3 15.6 1.0 NE1 A:TRP180 4.4 17.5 1.0 C5 A:INE760 4.6 22.4 1.0 N2 A:INE760 4.7 22.6 1.0 N1 A:INE760 4.7 25.6 1.0 BR A:INE760 4.8 24.3 1.0 C A:CYS186 4.8 14.9 1.0 N A:GLY188 4.8 19.2 1.0 C7 A:INE760 4.8 18.1 1.0 C6 A:INE760 4.9 17.7 1.0 N A:VAL187 4.9 16.9 1.0 CD1 A:TRP180 5.0 15.9 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 3- Bromo-7-Nitroindazole (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 3- Bromo-7-Nitroindazole (H4B Free) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:18.7 occ:1.00 FE B:HEM500 0.0 18.7 1.0 NB B:HEM500 2.0 21.7 1.0 ND B:HEM500 2.0 21.4 1.0 NC B:HEM500 2.0 17.0 1.0 NA B:HEM500 2.0 18.9 1.0 SG B:CYS186 2.4 21.7 1.0 C4C B:HEM500 3.0 19.9 1.0 C1B B:HEM500 3.0 17.4 1.0 C4A B:HEM500 3.0 23.4 1.0 C1C B:HEM500 3.0 23.4 1.0 C1D B:HEM500 3.1 21.7 1.0 C1A B:HEM500 3.1 21.5 1.0 C4B B:HEM500 3.1 18.2 1.0 C4D B:HEM500 3.1 20.7 1.0 CB B:CYS186 3.4 21.7 1.0 CHB B:HEM500 3.4 17.7 1.0 CHC B:HEM500 3.4 23.0 1.0 CHD B:HEM500 3.5 20.2 1.0 CHA B:HEM500 3.5 22.2 1.0 C9 B:INE761 4.0 23.2 1.0 C4 B:INE761 4.1 29.4 1.0 CA B:CYS186 4.1 21.4 1.0 C3 B:INE761 4.2 25.0 1.0 C3C B:HEM500 4.3 21.2 1.0 C2C B:HEM500 4.3 21.4 1.0 C3B B:HEM500 4.3 21.4 1.0 C2B B:HEM500 4.3 21.2 1.0 C3A B:HEM500 4.3 22.8 1.0 C2A B:HEM500 4.3 23.8 1.0 C2D B:HEM500 4.3 27.6 1.0 C3D B:HEM500 4.3 21.5 1.0 C8 B:INE761 4.3 19.9 1.0 NE1 B:TRP180 4.4 19.1 1.0 C5 B:INE761 4.6 22.4 1.0 N2 B:INE761 4.6 25.5 1.0 N1 B:INE761 4.7 25.1 1.0 C7 B:INE761 4.8 23.7 1.0 BR B:INE761 4.8 25.6 1.0 C B:CYS186 4.8 16.8 1.0 N B:GLY188 4.8 20.9 1.0 N B:VAL187 4.9 16.6 1.0 CD1 B:TRP180 5.0 19.1 1.0 C6 B:INE761 5.0 24.2 1.0

C.S.Raman, H.Li, P.Martasek, G.Southan, B.S.Masters, T.L.Poulos. Crystal Structure of Nitric Oxide Synthase Bound to Nitro Indazole Reveals A Novel Inactivation Mechanism. Biochemistry V. 40 13448 2001.
ISSN: ISSN 0006-2960
PubMed: 11695891
DOI: 10.1021/BI010957U