Iron in PDB 1d1x: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B Bound)

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B Bound):
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B Bound), PDB code: 1d1x 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)	36.61 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.530, 106.730, 156.730, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 25.4

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B 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 Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B Bound) (pdb code 1d1x). 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, 4-Pbitu (H4B Bound), PDB code: 1d1x:
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, 4-Pbitu (H4B 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 Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B Bound) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:28.9 occ:1.00 FE A:HEM500 0.0 28.9 1.0 NA A:HEM500 2.0 29.8 1.0 NC A:HEM500 2.0 28.3 1.0 NB A:HEM500 2.0 28.9 1.0 ND A:HEM500 2.0 29.3 1.0 SG A:CYS186 2.3 29.6 1.0 C1A A:HEM500 3.0 30.1 1.0 C1D A:HEM500 3.1 29.0 1.0 C4C A:HEM500 3.1 28.8 1.0 C4D A:HEM500 3.1 29.9 1.0 C1B A:HEM500 3.1 29.4 1.0 C4B A:HEM500 3.1 29.9 1.0 C4A A:HEM500 3.1 29.4 1.0 C1C A:HEM500 3.1 29.0 1.0 CB A:CYS186 3.3 29.6 1.0 CHD A:HEM500 3.4 29.0 1.0 CHA A:HEM500 3.5 28.7 1.0 CHC A:HEM500 3.5 28.5 1.0 CHB A:HEM500 3.5 28.2 1.0 CA A:4BT830 3.6 36.1 1.0 CA A:CYS186 4.0 29.9 1.0 C2A A:HEM500 4.3 30.1 1.0 C3C A:HEM500 4.3 28.1 1.0 C3D A:HEM500 4.3 29.7 1.0 C2D A:HEM500 4.3 30.4 1.0 C2C A:HEM500 4.3 29.1 1.0 C2B A:HEM500 4.3 29.5 1.0 C3A A:HEM500 4.3 29.5 1.0 C3B A:HEM500 4.4 29.6 1.0 NE1 A:TRP180 4.4 27.1 1.0 S A:4BT830 4.5 35.7 1.0 C2 A:4BT830 4.7 39.8 1.0 N A:GLY188 4.7 28.8 1.0 C A:4BT830 4.8 35.9 1.0 C A:CYS186 4.8 30.1 1.0 N2 A:4BT830 4.8 34.2 1.0 CB A:4BT830 4.8 37.0 1.0 N A:VAL187 4.8 29.1 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B 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 Nitric Oxide Synthase Heme Domain Complexed with 1, 4-Pbitu (H4B Bound) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:28.9 occ:1.00 FE B:HEM500 0.0 28.9 1.0 ND B:HEM500 2.0 28.6 1.0 NB B:HEM500 2.0 27.9 1.0 NC B:HEM500 2.0 28.6 1.0 NA B:HEM500 2.0 27.7 1.0 SG B:CYS186 2.3 28.7 1.0 C1D B:HEM500 3.0 28.8 1.0 C1B B:HEM500 3.0 28.2 1.0 C4A B:HEM500 3.1 27.7 1.0 C4D B:HEM500 3.1 28.9 1.0 C4B B:HEM500 3.1 27.9 1.0 C4C B:HEM500 3.1 27.8 1.0 C1C B:HEM500 3.1 29.2 1.0 C1A B:HEM500 3.1 28.0 1.0 CHD B:HEM500 3.4 29.3 1.0 CHB B:HEM500 3.4 28.1 1.0 CB B:CYS186 3.4 29.9 1.0 CHC B:HEM500 3.4 28.7 1.0 CHA B:HEM500 3.5 26.9 1.0 CA B:4BT831 3.6 35.1 1.0 CA B:CYS186 4.1 30.6 1.0 C3D B:HEM500 4.3 28.3 1.0 C2B B:HEM500 4.3 28.1 1.0 C2D B:HEM500 4.3 28.6 1.0 C3A B:HEM500 4.3 28.3 1.0 C2A B:HEM500 4.3 28.1 1.0 C2C B:HEM500 4.3 29.4 1.0 C3C B:HEM500 4.3 29.4 1.0 C3B B:HEM500 4.3 28.6 1.0 S B:4BT831 4.4 36.3 1.0 NE1 B:TRP180 4.4 27.8 1.0 C B:4BT831 4.7 32.6 1.0 CB B:4BT831 4.8 37.6 1.0 C2 B:4BT831 4.8 41.1 1.0 C B:CYS186 4.9 30.9 1.0 N B:VAL187 4.9 30.5 1.0 N B:GLY188 4.9 30.7 1.0 N2 B:4BT831 4.9 32.2 1.0 CD1 B:TRP180 5.0 29.0 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