Iron in PDB 1rs6: Rat Neuronal Nos Heme Domain with D-Lysine-D-Nitroarginine Amide Bound

All present enzymatic activity of Rat Neuronal Nos Heme Domain with D-Lysine-D-Nitroarginine Amide Bound:
1.14.13.39;

The structure of Rat Neuronal Nos Heme Domain with D-Lysine-D-Nitroarginine Amide Bound, PDB code: 1rs6 was solved by M.Flinspach, H.Li, J.Jamal, W.Yang, H.Huang, R.B.Silverman, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.08 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.590, 109.810, 164.670, 90.00, 90.00, 90.00
R / Rfree (%)	22.1 / 25.4

The structure of Rat Neuronal Nos Heme Domain with D-Lysine-D-Nitroarginine Amide 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 D-Lysine-D-Nitroarginine Amide Bound (pdb code 1rs6). 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 D-Lysine-D-Nitroarginine Amide Bound, PDB code: 1rs6:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Rat Neuronal Nos Heme Domain with D-Lysine-D-Nitroarginine Amide 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 D-Lysine-D-Nitroarginine Amide Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe750 b:25.1 occ:1.00 FE A:HEM750 0.0 25.1 1.0 ND A:HEM750 2.0 27.4 1.0 NA A:HEM750 2.0 27.1 1.0 NC A:HEM750 2.0 26.3 1.0 NB A:HEM750 2.0 26.8 1.0 SG A:CYS415 2.3 28.2 1.0 C4D A:HEM750 3.0 26.5 1.0 C4A A:HEM750 3.0 26.5 1.0 C1A A:HEM750 3.0 26.3 1.0 C1B A:HEM750 3.0 26.8 1.0 C1D A:HEM750 3.1 26.5 1.0 C4C A:HEM750 3.1 25.5 1.0 C1C A:HEM750 3.1 25.5 1.0 C4B A:HEM750 3.1 26.6 1.0 CB A:CYS415 3.3 27.1 1.0 CHA A:HEM750 3.4 26.7 1.0 CHB A:HEM750 3.4 27.0 1.0 CHD A:HEM750 3.4 26.2 1.0 CHC A:HEM750 3.5 27.1 1.0 CA A:CYS415 4.0 27.5 1.0 NH1 A:DP2792 4.0 35.3 1.0 C3D A:HEM750 4.3 26.1 1.0 CZ A:DP2792 4.3 35.2 1.0 C2A A:HEM750 4.3 25.8 1.0 C3A A:HEM750 4.3 26.6 1.0 C2D A:HEM750 4.3 27.0 1.0 C3C A:HEM750 4.3 26.5 1.0 C2B A:HEM750 4.3 26.9 1.0 C2C A:HEM750 4.3 26.1 1.0 C3B A:HEM750 4.3 27.4 1.0 NE1 A:TRP409 4.5 25.3 1.0 N1 A:DP2792 4.5 35.3 1.0 NE A:DP2792 4.6 35.1 1.0 C A:CYS415 4.7 27.0 1.0 CD A:DP2792 4.8 36.2 1.0 N A:VAL416 4.8 26.7 1.0 NH2 A:DP2792 4.8 33.6 1.0 N A:GLY417 4.9 26.2 1.0 O3 A:DP2792 4.9 36.4 1.0

Iron binding site 2 out of 2 in the Rat Neuronal Nos Heme Domain with D-Lysine-D-Nitroarginine Amide 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 D-Lysine-D-Nitroarginine Amide Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe750 b:23.0 occ:1.00 FE B:HEM750 0.0 23.0 1.0 ND B:HEM750 2.0 23.5 1.0 NC B:HEM750 2.0 22.8 1.0 NB B:HEM750 2.0 24.4 1.0 NA B:HEM750 2.0 24.2 1.0 SG B:CYS415 2.3 23.5 1.0 C1D B:HEM750 3.0 22.7 1.0 C4C B:HEM750 3.0 23.2 1.0 C4D B:HEM750 3.0 23.3 1.0 C1C B:HEM750 3.0 22.7 1.0 C4B B:HEM750 3.0 23.7 1.0 C1B B:HEM750 3.1 24.6 1.0 C1A B:HEM750 3.1 24.4 1.0 C4A B:HEM750 3.1 23.5 1.0 CB B:CYS415 3.4 22.7 1.0 CHD B:HEM750 3.4 23.4 1.0 CHA B:HEM750 3.4 23.9 1.0 CHC B:HEM750 3.4 23.1 1.0 CHB B:HEM750 3.5 23.3 1.0 NH1 B:DP2793 3.9 31.2 1.0 CA B:CYS415 4.1 23.0 1.0 CZ B:DP2793 4.2 31.7 1.0 C2D B:HEM750 4.2 22.8 1.0 C3C B:HEM750 4.2 23.2 1.0 C2C B:HEM750 4.2 22.9 1.0 C3D B:HEM750 4.3 23.8 1.0 C3B B:HEM750 4.3 25.4 1.0 C2B B:HEM750 4.3 24.2 1.0 C2A B:HEM750 4.3 24.3 1.0 C3A B:HEM750 4.3 23.7 1.0 NE1 B:TRP409 4.5 22.1 1.0 N1 B:DP2793 4.5 29.8 1.0 NE B:DP2793 4.5 32.5 1.0 CD B:DP2793 4.7 34.5 1.0 N B:GLY417 4.8 24.2 1.0 NH2 B:DP2793 4.8 30.0 1.0 C B:CYS415 4.9 24.0 1.0 O3 B:DP2793 5.0 29.4 1.0 N B:VAL416 5.0 23.6 1.0 O2 B:DP2793 5.0 30.9 1.0

M.Flinspach, H.Li, J.Jamal, W.Yang, H.Huang, R.B.Silverman, T.L.Poulos. Structures of the Neuronal and Endothelial Nitric Oxide Synthase Heme Domain with D-Nitroarginine-Containing Dipeptide Inhibitors Bound. Biochemistry V. 43 5181 2004.
ISSN: ISSN 0006-2960
PubMed: 15122883
DOI: 10.1021/BI0361867