Iron in PDB 1rs9: Bovine Endothelial Nos Heme Domain with D-Phenylalanine-D- Nitroarginine Amide Bound

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

The structure of Bovine Endothelial Nos Heme Domain with D-Phenylalanine-D- Nitroarginine Amide Bound, PDB code: 1rs9 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)	39.50 / 2.22
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.791, 106.647, 157.659, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 26.4

The structure of Bovine Endothelial Nos Heme Domain with D-Phenylalanine-D- Nitroarginine Amide Bound also contains other interesting chemical elements:

Arsenic	(As)	2 atoms
Zinc	(Zn)	1 atom

The binding sites of Iron atom in the Bovine Endothelial Nos Heme Domain with D-Phenylalanine-D- Nitroarginine Amide Bound (pdb code 1rs9). 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 Nos Heme Domain with D-Phenylalanine-D- Nitroarginine Amide Bound, PDB code: 1rs9:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Bovine Endothelial 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 Bovine Endothelial Nos Heme Domain with D-Phenylalanine-D- Nitroarginine Amide Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:33.2 occ:1.00 FE A:HEM500 0.0 33.2 1.0 NB A:HEM500 1.9 30.2 1.0 NA A:HEM500 2.0 33.5 1.0 ND A:HEM500 2.0 30.3 1.0 NC A:HEM500 2.0 32.3 1.0 SG A:CYS186 2.3 36.3 1.0 C1B A:HEM500 3.0 33.0 1.0 C4B A:HEM500 3.0 32.5 1.0 C1C A:HEM500 3.0 31.2 1.0 C1A A:HEM500 3.0 33.0 1.0 C4D A:HEM500 3.1 32.5 1.0 C4C A:HEM500 3.1 32.6 1.0 C4A A:HEM500 3.1 32.7 1.0 C1D A:HEM500 3.1 32.1 1.0 CHC A:HEM500 3.4 33.3 1.0 CB A:CYS186 3.4 34.4 1.0 CHA A:HEM500 3.4 32.1 1.0 CHB A:HEM500 3.4 31.7 1.0 CHD A:HEM500 3.5 30.2 1.0 CA A:CYS186 4.1 34.3 1.0 C2B A:HEM500 4.2 30.7 1.0 NH1 A:D7P797 4.3 41.6 1.0 CZ A:D7P797 4.3 38.4 1.0 C3B A:HEM500 4.3 32.8 1.0 C2A A:HEM500 4.3 33.8 1.0 C2C A:HEM500 4.3 33.3 1.0 C3C A:HEM500 4.3 32.8 1.0 NE1 A:TRP180 4.3 32.4 1.0 C3D A:HEM500 4.3 32.6 1.0 C3A A:HEM500 4.3 32.0 1.0 C2D A:HEM500 4.3 32.3 1.0 NO A:D7P797 4.4 42.8 1.0 NE A:D7P797 4.4 38.5 1.0 O2 A:D7P797 4.6 44.0 1.0 CD A:D7P797 4.7 37.8 1.0 NH2 A:D7P797 4.7 39.7 1.0 O3 A:D7P797 4.8 44.2 1.0 C A:CYS186 4.8 34.3 1.0 N A:GLY188 4.9 32.1 1.0 N A:VAL187 4.9 33.1 1.0 CD1 A:TRP180 5.0 32.4 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial 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 Bovine Endothelial Nos Heme Domain with D-Phenylalanine-D- Nitroarginine Amide Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:35.0 occ:1.00 FE B:HEM500 0.0 35.0 1.0 NB B:HEM500 2.0 31.6 1.0 ND B:HEM500 2.0 29.7 1.0 NC B:HEM500 2.0 30.7 1.0 NA B:HEM500 2.0 32.3 1.0 SG B:CYS186 2.2 32.8 1.0 C1C B:HEM500 3.0 31.1 1.0 C4D B:HEM500 3.0 32.2 1.0 C1B B:HEM500 3.0 31.4 1.0 C1A B:HEM500 3.1 31.1 1.0 C4B B:HEM500 3.1 32.2 1.0 C1D B:HEM500 3.1 31.4 1.0 C4A B:HEM500 3.1 34.0 1.0 C4C B:HEM500 3.1 29.9 1.0 CB B:CYS186 3.4 30.8 1.0 CHC B:HEM500 3.4 31.6 1.0 CHA B:HEM500 3.4 29.9 1.0 CHB B:HEM500 3.4 32.8 1.0 CHD B:HEM500 3.5 30.6 1.0 CA B:CYS186 4.1 32.1 1.0 NH1 B:D7P798 4.2 44.8 1.0 C2B B:HEM500 4.3 30.5 1.0 C2C B:HEM500 4.3 32.3 1.0 C3D B:HEM500 4.3 30.8 1.0 C2D B:HEM500 4.3 31.5 1.0 C3B B:HEM500 4.3 31.4 1.0 C3C B:HEM500 4.3 31.7 1.0 C3A B:HEM500 4.3 33.6 1.0 C2A B:HEM500 4.3 34.5 1.0 CZ B:D7P798 4.3 41.2 1.0 NE1 B:TRP180 4.4 32.4 1.0 NO B:D7P798 4.5 44.7 1.0 NE B:D7P798 4.5 41.3 1.0 CD B:D7P798 4.7 40.9 1.0 O2 B:D7P798 4.8 47.9 1.0 C B:CYS186 4.9 32.0 1.0 NH2 B:D7P798 4.9 41.2 1.0 N B:GLY188 4.9 34.0 1.0 N B:VAL187 4.9 32.6 1.0 O3 B:D7P798 4.9 45.7 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