Iron in PDB 1dmi: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 6S-H4B

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 6S-H4B:
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 6S-H4B, PDB code: 1dmi was solved by C.S.Raman, H.Li, P.Martasek, P.Kotsonis, W.Pfleiderer, H.H.H.W.Schmidt, 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)	32.59 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.630, 106.560, 156.790, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 26.4

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 6S-H4B 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 6S-H4B (pdb code 1dmi). 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 6S-H4B, PDB code: 1dmi:
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 6S-H4B


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 6S-H4B within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1500 b:30.0 occ:1.00 FE A:HEM1500 0.0 30.0 1.0 NC A:HEM1500 2.0 33.3 1.0 NA A:HEM1500 2.0 35.3 1.0 NB A:HEM1500 2.0 32.6 1.0 ND A:HEM1500 2.0 34.0 1.0 SG A:CYS186 2.3 34.5 1.0 C1D A:HEM1500 3.0 34.5 1.0 C4C A:HEM1500 3.0 33.9 1.0 C1B A:HEM1500 3.1 33.8 1.0 C4D A:HEM1500 3.1 35.6 1.0 C1A A:HEM1500 3.1 36.2 1.0 C1C A:HEM1500 3.1 33.7 1.0 C4A A:HEM1500 3.1 34.9 1.0 C4B A:HEM1500 3.1 33.4 1.0 CB A:CYS186 3.3 33.1 1.0 CHD A:HEM1500 3.4 34.3 1.0 CHB A:HEM1500 3.4 34.5 1.0 CHA A:HEM1500 3.5 34.8 1.0 CHC A:HEM1500 3.5 33.1 1.0 C2 A:ITU1800 3.9 40.5 1.0 S A:ITU1800 4.0 40.1 1.0 CA A:CYS186 4.0 34.3 1.0 C3D A:HEM1500 4.3 35.5 1.0 C2D A:HEM1500 4.3 35.9 1.0 C3C A:HEM1500 4.3 33.2 1.0 C2C A:HEM1500 4.3 33.1 1.0 C2A A:HEM1500 4.3 37.5 1.0 C3A A:HEM1500 4.3 36.9 1.0 C2B A:HEM1500 4.3 32.7 1.0 C3B A:HEM1500 4.4 33.0 1.0 NE1 A:TRP180 4.4 32.8 1.0 C3 A:ITU1800 4.4 39.2 1.0 N1 A:ITU1800 4.6 37.6 1.0 O A:HOH1970 4.6 50.7 1.0 C A:CYS186 4.8 34.5 1.0 N A:GLY188 4.8 35.1 1.0 N A:VAL187 4.9 34.7 1.0 CD1 A:TRP180 5.0 31.2 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with 6S-H4B


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 6S-H4B within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2500 b:35.7 occ:1.00 FE B:HEM2500 0.0 35.7 1.0 ND B:HEM2500 2.0 36.3 1.0 NC B:HEM2500 2.0 35.0 1.0 NB B:HEM2500 2.0 34.2 1.0 NA B:HEM2500 2.0 35.8 1.0 SG B:CYS186 2.3 36.4 1.0 C1D B:HEM2500 3.0 35.6 1.0 C4C B:HEM2500 3.0 34.8 1.0 C4D B:HEM2500 3.1 36.7 1.0 C1C B:HEM2500 3.1 34.8 1.0 C1B B:HEM2500 3.1 35.8 1.0 C4B B:HEM2500 3.1 35.6 1.0 C1A B:HEM2500 3.1 36.1 1.0 C4A B:HEM2500 3.1 35.0 1.0 CB B:CYS186 3.4 36.3 1.0 CHD B:HEM2500 3.4 35.4 1.0 CHC B:HEM2500 3.5 34.0 1.0 CHA B:HEM2500 3.5 36.3 1.0 CHB B:HEM2500 3.5 34.7 1.0 C2 B:ITU2800 3.8 44.5 1.0 S B:ITU2800 4.0 47.6 1.0 CA B:CYS186 4.1 36.4 1.0 C2D B:HEM2500 4.3 35.9 1.0 C3D B:HEM2500 4.3 37.2 1.0 C2C B:HEM2500 4.3 35.4 1.0 C3C B:HEM2500 4.3 34.5 1.0 C2B B:HEM2500 4.3 35.4 1.0 C3B B:HEM2500 4.3 35.0 1.0 C3A B:HEM2500 4.3 35.3 1.0 C2A B:HEM2500 4.3 36.5 1.0 NE1 B:TRP180 4.3 34.4 1.0 N1 B:ITU2800 4.5 45.9 1.0 C3 B:ITU2800 4.5 46.6 1.0 C B:CYS186 4.8 35.8 1.0 N B:VAL187 4.9 35.8 1.0 N B:GLY188 4.9 37.6 1.0

C.S.Raman, H.Li, P.Martasek, P.Kotsonis, W.Pfleiderer, H.H.H.W.Schmidt, G.J.Southan, B.S.S.Masters, T.L.Poulos. Crystal Structures of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with the Pterin Analogues To Be Published.