Iron in PDB 1om5: Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7- Nitroindazole Bound

All present enzymatic activity of Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7- Nitroindazole Bound:
1.14.13.39;

The structure of Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7- Nitroindazole Bound, PDB code: 1om5 was solved by H.Li, P.Martasek, B.S.S.Masters, T.L.Poulos, C.S.Raman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.56 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.700, 110.780, 164.580, 90.00, 90.00, 90.00
R / Rfree (%)	23.1 / 28

The structure of Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7- Nitroindazole Bound also contains other interesting chemical elements:

Bromine	(Br)	2 atoms
Zinc	(Zn)	1 atom

The binding sites of Iron atom in the Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7- Nitroindazole Bound (pdb code 1om5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7- Nitroindazole Bound, PDB code: 1om5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7- Nitroindazole Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7- Nitroindazole Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe750 b:38.9 occ:1.00 FE A:HEM750 0.0 38.9 1.0 NB A:HEM750 2.0 38.5 1.0 NC A:HEM750 2.0 36.0 1.0 NA A:HEM750 2.0 38.3 1.0 ND A:HEM750 2.0 36.3 1.0 SG A:CYS415 2.2 42.3 1.0 C1B A:HEM750 3.0 40.1 1.0 C4B A:HEM750 3.0 38.8 1.0 C1C A:HEM750 3.0 37.5 1.0 C4A A:HEM750 3.0 37.9 1.0 C4C A:HEM750 3.1 35.2 1.0 C4D A:HEM750 3.1 36.8 1.0 C1D A:HEM750 3.1 35.0 1.0 C1A A:HEM750 3.1 39.1 1.0 CB A:CYS415 3.3 37.1 1.0 CHB A:HEM750 3.4 39.8 1.0 CHC A:HEM750 3.4 39.4 1.0 CHD A:HEM750 3.5 36.2 1.0 CHA A:HEM750 3.5 37.8 1.0 CA A:CYS415 4.0 37.4 1.0 C3 A:INE790 4.1 45.5 1.0 C9 A:INE790 4.2 48.5 1.0 C2B A:HEM750 4.3 41.2 1.0 C3B A:HEM750 4.3 40.0 1.0 C3D A:HEM750 4.3 38.6 1.0 C3A A:HEM750 4.3 38.1 1.0 C2C A:HEM750 4.3 37.0 1.0 C3C A:HEM750 4.3 36.2 1.0 N2 A:INE790 4.3 49.8 1.0 C2D A:HEM750 4.3 37.6 1.0 C2A A:HEM750 4.3 40.7 1.0 C8 A:INE790 4.4 48.6 1.0 N1 A:INE790 4.5 50.4 1.0 NE1 A:TRP409 4.6 32.5 1.0 C4 A:INE790 4.7 52.2 1.0 BR A:INE790 4.8 51.6 1.0 C A:CYS415 4.8 36.6 1.0 N A:VAL416 4.9 38.0 1.0

Iron binding site 2 out of 2 in the Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7- Nitroindazole Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7- Nitroindazole Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe750 b:33.6 occ:1.00 FE B:HEM750 0.0 33.6 1.0 NA B:HEM750 1.9 29.3 1.0 NC B:HEM750 1.9 29.7 1.0 NB B:HEM750 1.9 29.8 1.0 ND B:HEM750 2.0 31.1 1.0 SG B:CYS415 2.2 37.5 1.0 C1A B:HEM750 3.0 35.0 1.0 C4D B:HEM750 3.0 33.0 1.0 C1C B:HEM750 3.0 32.8 1.0 C4A B:HEM750 3.0 34.5 1.0 C4C B:HEM750 3.0 31.4 1.0 C4B B:HEM750 3.0 30.0 1.0 C1D B:HEM750 3.0 34.7 1.0 C1B B:HEM750 3.0 34.3 1.0 CHA B:HEM750 3.4 32.8 1.0 CHC B:HEM750 3.4 30.8 1.0 CHB B:HEM750 3.4 34.4 1.0 CHD B:HEM750 3.4 34.7 1.0 CB B:CYS415 3.5 33.3 1.0 C3 B:INE791 4.1 50.4 1.0 C9 B:INE791 4.2 52.1 1.0 C2A B:HEM750 4.2 33.2 1.0 C3A B:HEM750 4.2 30.7 1.0 C3D B:HEM750 4.2 34.9 1.0 C2C B:HEM750 4.2 32.6 1.0 C3C B:HEM750 4.2 31.5 1.0 CA B:CYS415 4.2 33.2 1.0 C2D B:HEM750 4.3 33.2 1.0 C2B B:HEM750 4.3 27.9 1.0 C3B B:HEM750 4.3 27.2 1.0 N2 B:INE791 4.5 53.7 1.0 C8 B:INE791 4.5 53.9 1.0 C4 B:INE791 4.5 52.0 1.0 NE1 B:TRP409 4.6 25.2 1.0 N1 B:INE791 4.7 53.8 1.0 BR B:INE791 4.8 52.7 1.0 N B:GLY417 5.0 39.2 1.0 C B:CYS415 5.0 37.4 1.0

H.Li, P.Martasek, B.S.S.Masters, T.L.Poulos, C.S.Raman. Structure of Rat Neuronal Nos Heme Domain with 3-Bromo-7-Nitroindazole Bound To Be Published.