Iron in PDB 1rs7: Rat Neuronal Nos Heme Domain with D-Phenylalanine-D-Nitroarginine Amide Bound

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

The structure of Rat Neuronal Nos Heme Domain with D-Phenylalanine-D-Nitroarginine Amide Bound, PDB code: 1rs7 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)	39.06 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.085, 110.909, 165.032, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 25.1

The structure of Rat Neuronal Nos Heme Domain with D-Phenylalanine-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-Phenylalanine-D-Nitroarginine Amide Bound (pdb code 1rs7). 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-Phenylalanine-D-Nitroarginine Amide Bound, PDB code: 1rs7:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Rat Neuronal Nos Heme Domain with D-Phenylalanine-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-Phenylalanine-D-Nitroarginine Amide Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe750 b:19.5 occ:1.00 FE A:HEM750 0.0 19.5 1.0 NC A:HEM750 2.0 20.4 1.0 ND A:HEM750 2.0 20.8 1.0 NB A:HEM750 2.0 20.4 1.0 NA A:HEM750 2.0 20.3 1.0 SG A:CYS415 2.2 21.0 1.0 C1C A:HEM750 3.0 20.5 1.0 C4D A:HEM750 3.0 20.5 1.0 C4C A:HEM750 3.1 21.0 1.0 C4B A:HEM750 3.1 20.6 1.0 C1D A:HEM750 3.1 20.8 1.0 C1B A:HEM750 3.1 20.2 1.0 C4A A:HEM750 3.1 20.0 1.0 C1A A:HEM750 3.1 19.7 1.0 CHC A:HEM750 3.4 20.8 1.0 CHA A:HEM750 3.4 20.5 1.0 CB A:CYS415 3.4 20.4 1.0 CHD A:HEM750 3.5 20.8 1.0 CHB A:HEM750 3.5 20.2 1.0 NH1 A:D7P797 4.1 31.5 1.0 CA A:CYS415 4.1 20.0 1.0 C3D A:HEM750 4.3 20.4 1.0 C2C A:HEM750 4.3 21.0 1.0 C3C A:HEM750 4.3 21.2 1.0 C3B A:HEM750 4.3 20.8 1.0 C2D A:HEM750 4.3 20.9 1.0 C2B A:HEM750 4.3 20.4 1.0 C3A A:HEM750 4.3 20.4 1.0 CZ A:D7P797 4.4 32.2 1.0 C2A A:HEM750 4.4 20.1 1.0 NE1 A:TRP409 4.4 19.2 1.0 NO A:D7P797 4.5 31.8 1.0 NE A:D7P797 4.6 32.0 1.0 N A:GLY417 4.8 20.1 1.0 O3 A:D7P797 4.8 31.4 1.0 CD A:D7P797 4.9 32.8 1.0 NH2 A:D7P797 4.9 31.3 1.0 C A:CYS415 4.9 20.0 1.0 O2 A:D7P797 5.0 32.2 1.0 N A:VAL416 5.0 19.5 1.0

Iron binding site 2 out of 2 in the Rat Neuronal Nos Heme Domain with D-Phenylalanine-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-Phenylalanine-D-Nitroarginine Amide Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe750 b:18.3 occ:1.00 FE B:HEM750 0.0 18.3 1.0 NC B:HEM750 2.0 17.9 1.0 NB B:HEM750 2.0 18.2 1.0 NA B:HEM750 2.0 18.2 1.0 ND B:HEM750 2.0 17.9 1.0 SG B:CYS415 2.2 18.6 1.0 C1C B:HEM750 3.0 18.3 1.0 C4B B:HEM750 3.0 18.7 1.0 C1B B:HEM750 3.0 18.9 1.0 C1D B:HEM750 3.1 18.5 1.0 C4C B:HEM750 3.1 18.7 1.0 C4D B:HEM750 3.1 18.3 1.0 C1A B:HEM750 3.1 18.6 1.0 C4A B:HEM750 3.1 18.0 1.0 CB B:CYS415 3.3 18.2 1.0 CHC B:HEM750 3.4 18.4 1.0 CHB B:HEM750 3.4 18.6 1.0 CHA B:HEM750 3.5 18.2 1.0 CHD B:HEM750 3.5 17.9 1.0 NH1 B:D7P798 4.1 32.0 1.0 CA B:CYS415 4.1 18.7 1.0 C2C B:HEM750 4.3 18.9 1.0 CZ B:D7P798 4.3 31.9 1.0 C3B B:HEM750 4.3 19.4 1.0 C2B B:HEM750 4.3 18.8 1.0 C3A B:HEM750 4.3 18.3 1.0 C3C B:HEM750 4.3 18.9 1.0 C2A B:HEM750 4.3 18.6 1.0 C2D B:HEM750 4.3 18.1 1.0 C3D B:HEM750 4.3 18.3 1.0 NE1 B:TRP409 4.4 18.1 1.0 NO B:D7P798 4.4 32.5 1.0 NE B:D7P798 4.5 31.3 1.0 O2 B:D7P798 4.7 32.8 1.0 NH2 B:D7P798 4.7 31.8 1.0 N B:GLY417 4.8 18.3 1.0 CD B:D7P798 4.8 30.8 1.0 C B:CYS415 4.9 18.7 1.0 O3 B:D7P798 4.9 32.0 1.0 N B:VAL416 5.0 18.4 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