Iron in PDB 1m00: Rat Neuronal Nos Heme Domain with N-Butyl-N'-Hydroxyguanidine Bound

All present enzymatic activity of Rat Neuronal Nos Heme Domain with N-Butyl-N'-Hydroxyguanidine Bound:
1.14.13.39;

The structure of Rat Neuronal Nos Heme Domain with N-Butyl-N'-Hydroxyguanidine Bound, PDB code: 1m00 was solved by H.Li, H.Shimizu, M.Flinspach, J.Jamal, W.Yang, M.Xian, T.Cai, E.Z.Wen, Q.Jia, P.G.Wang, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.03 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.070, 111.250, 163.840, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 27

The structure of Rat Neuronal Nos Heme Domain with N-Butyl-N'-Hydroxyguanidine Bound also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Iron atom in the Rat Neuronal Nos Heme Domain with N-Butyl-N'-Hydroxyguanidine Bound (pdb code 1m00). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Rat Neuronal Nos Heme Domain with N-Butyl-N'-Hydroxyguanidine Bound, PDB code: 1m00:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Rat Neuronal Nos Heme Domain with N-Butyl-N'-Hydroxyguanidine Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rat Neuronal Nos Heme Domain with N-Butyl-N'-Hydroxyguanidine Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe750 b:21.5 occ:1.00 FE A:HEM750 0.0 21.5 1.0 NA A:HEM750 1.9 22.1 1.0 NC A:HEM750 2.0 21.5 1.0 ND A:HEM750 2.0 21.8 1.0 NB A:HEM750 2.0 22.1 1.0 SG A:CYS415 2.2 22.4 1.0 C4C A:HEM750 3.0 21.4 1.0 C4A A:HEM750 3.0 21.9 1.0 C1A A:HEM750 3.0 22.0 1.0 C1C A:HEM750 3.0 21.4 1.0 C4D A:HEM750 3.1 21.8 1.0 C1D A:HEM750 3.1 21.5 1.0 C4B A:HEM750 3.1 21.9 1.0 C1B A:HEM750 3.1 21.9 1.0 CB A:CYS415 3.3 22.1 1.0 CHC A:HEM750 3.4 21.7 1.0 CHD A:HEM750 3.4 21.6 1.0 CHB A:HEM750 3.4 21.7 1.0 CHA A:HEM750 3.4 21.7 1.0 NH1 A:BHH831 4.0 36.0 1.0 CA A:CYS415 4.1 21.8 1.0 C3C A:HEM750 4.2 21.4 1.0 C3A A:HEM750 4.2 22.2 1.0 C2A A:HEM750 4.3 22.0 1.0 C3D A:HEM750 4.3 21.8 1.0 C2D A:HEM750 4.3 21.5 1.0 C2C A:HEM750 4.3 21.3 1.0 C3B A:HEM750 4.3 22.2 1.0 C2B A:HEM750 4.3 22.3 1.0 OH A:BHH831 4.4 36.0 1.0 NE1 A:TRP409 4.5 21.6 1.0 CZ A:BHH831 4.5 35.8 1.0 C A:CYS415 4.8 21.6 1.0 N A:GLY417 4.8 22.2 1.0 N A:VAL416 4.9 21.3 1.0 NE A:BHH831 4.9 35.8 1.0

Iron binding site 2 out of 2 in the Rat Neuronal Nos Heme Domain with N-Butyl-N'-Hydroxyguanidine Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Rat Neuronal Nos Heme Domain with N-Butyl-N'-Hydroxyguanidine Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe750 b:19.7 occ:1.00 FE B:HEM750 0.0 19.7 1.0 NC B:HEM750 2.0 19.5 1.0 ND B:HEM750 2.0 19.7 1.0 NA B:HEM750 2.0 19.9 1.0 NB B:HEM750 2.0 20.0 1.0 SG B:CYS415 2.2 20.4 1.0 C4D B:HEM750 3.0 19.8 1.0 C1C B:HEM750 3.0 19.7 1.0 C4C B:HEM750 3.0 19.5 1.0 C1A B:HEM750 3.0 19.9 1.0 C1D B:HEM750 3.0 19.4 1.0 C4B B:HEM750 3.0 20.2 1.0 C4A B:HEM750 3.1 19.8 1.0 C1B B:HEM750 3.1 20.1 1.0 CB B:CYS415 3.4 20.3 1.0 CHC B:HEM750 3.4 19.5 1.0 CHA B:HEM750 3.4 19.7 1.0 CHD B:HEM750 3.4 19.5 1.0 CHB B:HEM750 3.6 19.9 1.0 NH1 B:BHH1831 4.0 35.1 1.0 CA B:CYS415 4.2 20.6 1.0 C2C B:HEM750 4.2 19.9 1.0 C3C B:HEM750 4.2 19.8 1.0 C3D B:HEM750 4.2 20.1 1.0 C2A B:HEM750 4.2 19.9 1.0 C2D B:HEM750 4.3 19.6 1.0 C3A B:HEM750 4.3 19.8 1.0 C3B B:HEM750 4.3 20.5 1.0 CZ B:BHH1831 4.4 35.4 1.0 C2B B:HEM750 4.4 20.4 1.0 NE1 B:TRP409 4.4 18.6 1.0 OH B:BHH1831 4.5 34.6 1.0 NE B:BHH1831 4.7 35.5 1.0 N B:GLY417 4.8 20.8 1.0 C B:CYS415 4.9 20.5 1.0 C1 B:BHH1831 4.9 35.7 1.0 NH2 B:BHH1831 4.9 34.7 1.0

H.Li, H.Shimizu, M.Flinspach, J.Jamal, W.Yang, M.Xian, T.Cai, E.Z.Wen, Q.Jia, P.G.Wang, T.L.Poulos. The Novel Binding Mode of N-Alkyl-N'-Hydroxyguanidine to Neuronal Nitric Oxide Synthase Provides Mechanistic Insights Into No Biosynthesis Biochemistry V. 41 13868 2002.
ISSN: ISSN 0006-2960
PubMed: 12437343
DOI: 10.1021/BI020417C