Iron in PDB 1p6l: Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound

All present enzymatic activity of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound:
1.14.13.39;

The structure of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound, PDB code: 1p6l was solved by M.L.Flinspach, H.Li, J.Jamal, W.Yang, H.Huang, J.-M.Hah, J.A.Gomez-Vidal, E.A.Litzinger, 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)	34.98 / 2.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.773, 106.243, 156.487, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 27.2

The structure of Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric 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 L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound (pdb code 1p6l). 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 L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound, PDB code: 1p6l:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric 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 L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:27.9 occ:1.00 FE A:HEM500 0.0 27.9 1.0 NC A:HEM500 2.0 27.6 1.0 NA A:HEM500 2.0 27.1 1.0 NB A:HEM500 2.0 26.1 1.0 ND A:HEM500 2.0 28.1 1.0 SG A:CYS186 2.2 29.5 1.0 C4C A:HEM500 3.0 28.1 1.0 C1B A:HEM500 3.0 24.8 1.0 C1C A:HEM500 3.0 27.7 1.0 C1A A:HEM500 3.1 27.8 1.0 C4A A:HEM500 3.1 27.1 1.0 C4B A:HEM500 3.1 26.7 1.0 C4D A:HEM500 3.1 28.7 1.0 C1D A:HEM500 3.1 27.0 1.0 CB A:CYS186 3.3 31.4 1.0 CHB A:HEM500 3.4 25.9 1.0 CHD A:HEM500 3.4 27.5 1.0 CHC A:HEM500 3.4 27.3 1.0 CHA A:HEM500 3.5 27.7 1.0 CA A:CYS186 4.1 30.8 1.0 NH1 A:DP1790 4.2 36.4 1.0 C2B A:HEM500 4.3 25.0 1.0 C2C A:HEM500 4.3 27.6 1.0 C3C A:HEM500 4.3 28.3 1.0 C2A A:HEM500 4.3 28.1 1.0 C3B A:HEM500 4.3 25.5 1.0 C3D A:HEM500 4.3 29.3 1.0 C2D A:HEM500 4.3 29.2 1.0 NO A:DP1790 4.3 34.9 1.0 C3A A:HEM500 4.3 27.7 1.0 NE1 A:TRP180 4.5 28.4 1.0 O2 A:DP1790 4.6 34.5 1.0 O3 A:DP1790 4.6 33.4 1.0 CZ A:DP1790 4.8 37.5 1.0 N A:GLY188 4.8 30.1 1.0 C A:CYS186 4.9 30.8 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nos Heme Domain with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric 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 L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:31.2 occ:1.00 FE B:HEM500 0.0 31.2 1.0 ND B:HEM500 2.0 30.8 1.0 NA B:HEM500 2.0 30.6 1.0 NC B:HEM500 2.0 29.1 1.0 NB B:HEM500 2.0 29.7 1.0 SG B:CYS186 2.2 29.6 1.0 C1D B:HEM500 3.0 30.8 1.0 C4D B:HEM500 3.0 31.2 1.0 C1A B:HEM500 3.1 31.3 1.0 C4C B:HEM500 3.1 30.0 1.0 C1C B:HEM500 3.1 29.8 1.0 C4B B:HEM500 3.1 30.3 1.0 C1B B:HEM500 3.1 29.8 1.0 C4A B:HEM500 3.1 30.3 1.0 CB B:CYS186 3.4 29.8 1.0 CHD B:HEM500 3.4 31.2 1.0 CHC B:HEM500 3.4 29.9 1.0 CHA B:HEM500 3.5 30.7 1.0 CHB B:HEM500 3.5 30.2 1.0 CA B:CYS186 4.1 29.1 1.0 NH1 B:DP1791 4.2 48.8 1.0 C2D B:HEM500 4.3 30.6 1.0 C3D B:HEM500 4.3 31.3 1.0 C2A B:HEM500 4.3 31.8 1.0 C2C B:HEM500 4.3 30.0 1.0 C2B B:HEM500 4.3 29.5 1.0 C3A B:HEM500 4.3 30.3 1.0 C3B B:HEM500 4.3 30.3 1.0 C3C B:HEM500 4.3 30.7 1.0 NO B:DP1791 4.4 49.1 1.0 NE1 B:TRP180 4.4 31.4 1.0 CZ B:DP1791 4.5 48.3 1.0 O2 B:DP1791 4.5 49.4 1.0 NH2 B:DP1791 4.7 48.8 1.0 N B:GLY188 4.8 28.4 1.0 C B:CYS186 4.9 29.5 1.0 O3 B:DP1791 4.9 49.3 1.0 N B:VAL187 4.9 29.4 1.0 CD1 B:TRP180 5.0 31.6 1.0

M.L.Flinspach, H.Li, J.Jamal, W.Yang, H.Huang, J.M.Hah, J.A.Gomez-Vidal, E.A.Litzinger, R.B.Silverman, T.L.Poulos. Structural Basis For Dipeptide Amide Isoform-Selective Inhibition of Neuronal Nitric Oxide Synthase. Nat.Struct.Mol.Biol. V. 11 54 2004.
ISSN: ISSN 1545-9993
PubMed: 14718923
DOI: 10.1038/NSMB704