Iron in PDB 1d1y: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free)

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free):
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free), PDB code: 1d1y was solved by C.S.Raman, H.Li, P.Martasek, G.J.Southan, B.S.S.Masters, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.32 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.660, 106.250, 156.440, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 26.8

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free) also contains other interesting chemical elements:

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

The binding sites of Iron atom in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free) (pdb code 1d1y). 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 Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free), PDB code: 1d1y:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:35.1 occ:1.00 FE A:HEM500 0.0 35.1 1.0 NA A:HEM500 2.0 34.6 1.0 NC A:HEM500 2.0 33.3 1.0 NB A:HEM500 2.0 32.5 1.0 ND A:HEM500 2.0 34.1 1.0 SG A:CYS186 2.3 36.0 1.0 C1A A:HEM500 3.0 37.4 1.0 C4C A:HEM500 3.0 34.3 1.0 C4A A:HEM500 3.1 35.4 1.0 C1B A:HEM500 3.1 31.0 1.0 C1C A:HEM500 3.1 33.0 1.0 C4D A:HEM500 3.1 35.1 1.0 C1D A:HEM500 3.1 32.7 1.0 C4B A:HEM500 3.1 32.7 1.0 CB A:CYS186 3.2 34.9 1.0 CHD A:HEM500 3.4 33.6 1.0 CHB A:HEM500 3.4 32.7 1.0 CHA A:HEM500 3.5 35.9 1.0 CHC A:HEM500 3.5 33.2 1.0 CA A:3BT820 3.7 49.0 1.0 CA A:CYS186 4.0 34.4 1.0 S A:3BT820 4.3 45.6 1.0 C2A A:HEM500 4.3 39.2 1.0 C3A A:HEM500 4.3 37.9 1.0 C2C A:HEM500 4.3 34.2 1.0 C3C A:HEM500 4.3 34.7 1.0 C2B A:HEM500 4.3 32.4 1.0 C3D A:HEM500 4.3 36.7 1.0 C3B A:HEM500 4.3 33.1 1.0 C2D A:HEM500 4.3 35.7 1.0 NE1 A:TRP180 4.4 30.8 1.0 C A:3BT820 4.6 46.3 1.0 N2 A:3BT820 4.7 44.6 1.0 C A:CYS186 4.8 34.1 1.0 N A:GLY188 5.0 31.1 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 3-Pbitu (H4B Free) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:29.7 occ:1.00 FE B:HEM500 0.0 29.7 1.0 NB B:HEM500 2.0 29.5 1.0 ND B:HEM500 2.0 31.9 1.0 NC B:HEM500 2.0 30.8 1.0 NA B:HEM500 2.0 32.5 1.0 SG B:CYS186 2.3 33.8 1.0 C1B B:HEM500 3.0 30.5 1.0 C1D B:HEM500 3.0 32.1 1.0 C4B B:HEM500 3.0 30.9 1.0 C4C B:HEM500 3.1 31.1 1.0 C1C B:HEM500 3.1 31.6 1.0 C4D B:HEM500 3.1 33.9 1.0 C4A B:HEM500 3.1 32.5 1.0 C1A B:HEM500 3.1 34.0 1.0 CHD B:HEM500 3.4 31.2 1.0 CB B:CYS186 3.4 33.7 1.0 CHB B:HEM500 3.4 32.1 1.0 CHC B:HEM500 3.4 30.6 1.0 CHA B:HEM500 3.5 32.8 1.0 CA B:3BT821 3.8 54.5 1.0 CA B:CYS186 4.1 33.6 1.0 S B:3BT821 4.2 53.7 1.0 C2B B:HEM500 4.2 29.3 1.0 C2D B:HEM500 4.3 32.5 1.0 C2C B:HEM500 4.3 31.9 1.0 C3B B:HEM500 4.3 30.4 1.0 C3C B:HEM500 4.3 31.1 1.0 C3D B:HEM500 4.3 33.8 1.0 C3A B:HEM500 4.3 34.5 1.0 C2A B:HEM500 4.4 35.2 1.0 NE1 B:TRP180 4.4 33.7 1.0 C B:3BT821 4.6 51.7 1.0 N2 B:3BT821 4.6 49.6 1.0 C B:CYS186 4.8 33.9 1.0 N B:VAL187 4.9 33.7 1.0 N B:GLY188 4.9 32.5 1.0

C.S.Raman, H.Li, P.Martasek, B.R.Babu, O.W.Griffith, B.S.Masters, T.L.Poulos. Implications For Isoform-Selective Inhibitor Design Derived From the Binding Mode of Bulky Isothioureas to the Heme Domain of Endothelial Nitric-Oxide Synthase. J.Biol.Chem. V. 276 26486 2001.
ISSN: ISSN 0021-9258
PubMed: 11331290
DOI: 10.1074/JBC.M102255200