Iron in PDB 1ed4: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with Ipitu (H4B Free)

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with Ipitu (H4B Free):
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with Ipitu (H4B Free), PDB code: 1ed4 was solved by C.S.Raman, H.Li, P.Martasek, V.Kral, 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)	36.73 / 1.86
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.028, 106.789, 156.461, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 23.5

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with Ipitu (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 Ipitu (H4B Free) (pdb code 1ed4). 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 Ipitu (H4B Free), PDB code: 1ed4:
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 Ipitu (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 Ipitu (H4B Free) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1500 b:21.9 occ:1.00 FE A:HEM1500 0.0 21.9 1.0 ND A:HEM1500 2.0 22.3 1.0 NA A:HEM1500 2.0 23.1 1.0 NB A:HEM1500 2.0 22.2 1.0 NC A:HEM1500 2.0 21.7 1.0 SG A:CYS186 2.3 21.9 1.0 C1A A:HEM1500 3.1 22.6 1.0 C4D A:HEM1500 3.1 23.3 1.0 C1D A:HEM1500 3.1 23.3 1.0 C1B A:HEM1500 3.1 22.8 1.0 C4A A:HEM1500 3.1 22.7 1.0 C4B A:HEM1500 3.1 22.0 1.0 C4C A:HEM1500 3.1 22.1 1.0 C1C A:HEM1500 3.1 21.7 1.0 CB A:CYS186 3.3 22.0 1.0 CHA A:HEM1500 3.4 23.1 1.0 CHB A:HEM1500 3.5 22.8 1.0 CHD A:HEM1500 3.5 22.9 1.0 CHC A:HEM1500 3.5 22.2 1.0 C3 A:IPU1830 3.9 22.4 1.0 CA A:CYS186 4.0 21.4 1.0 S A:IPU1830 4.2 24.6 1.0 C2A A:HEM1500 4.3 23.3 1.0 C2D A:HEM1500 4.3 23.8 1.0 C3D A:HEM1500 4.3 24.1 1.0 C2B A:HEM1500 4.3 22.6 1.0 C3A A:HEM1500 4.3 23.2 1.0 C3B A:HEM1500 4.3 22.7 1.0 C2C A:HEM1500 4.3 21.6 1.0 C3C A:HEM1500 4.4 22.2 1.0 NE1 A:TRP180 4.4 21.8 1.0 C A:IPU1830 4.6 23.4 1.0 C2 A:IPU1830 4.7 22.7 1.0 C A:CYS186 4.8 21.6 1.0 N A:GLY188 4.8 22.6 1.0 N A:VAL187 4.9 21.4 1.0 N1 A:IPU1830 5.0 22.7 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with Ipitu (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 Ipitu (H4B Free) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2500 b:22.0 occ:1.00 FE B:HEM2500 0.0 22.0 1.0 ND B:HEM2500 2.0 23.5 1.0 NB B:HEM2500 2.0 23.0 1.0 NC B:HEM2500 2.0 22.7 1.0 NA B:HEM2500 2.0 23.8 1.0 SG B:CYS186 2.3 23.2 1.0 C1D B:HEM2500 3.1 23.3 1.0 C1C B:HEM2500 3.1 23.0 1.0 C1B B:HEM2500 3.1 23.1 1.0 C4D B:HEM2500 3.1 24.0 1.0 C4C B:HEM2500 3.1 22.7 1.0 C4B B:HEM2500 3.1 23.2 1.0 C4A B:HEM2500 3.1 23.4 1.0 C1A B:HEM2500 3.1 24.1 1.0 CB B:CYS186 3.3 22.6 1.0 CHC B:HEM2500 3.4 23.3 1.0 CHD B:HEM2500 3.5 23.1 1.0 CHB B:HEM2500 3.5 23.1 1.0 CHA B:HEM2500 3.5 24.4 1.0 C3 B:IPU2830 3.9 23.6 1.0 CA B:CYS186 4.1 22.2 1.0 S B:IPU2830 4.2 24.5 1.0 C2D B:HEM2500 4.3 24.1 1.0 C3D B:HEM2500 4.3 24.7 1.0 C2B B:HEM2500 4.3 23.7 1.0 C2C B:HEM2500 4.3 22.9 1.0 C3A B:HEM2500 4.3 23.7 1.0 C3C B:HEM2500 4.3 23.3 1.0 C3B B:HEM2500 4.3 23.7 1.0 C2A B:HEM2500 4.3 24.3 1.0 NE1 B:TRP180 4.4 23.1 1.0 C B:IPU2830 4.6 23.9 1.0 C2 B:IPU2830 4.7 23.2 1.0 C B:CYS186 4.8 21.9 1.0 N B:GLY188 4.9 22.5 1.0 N B:VAL187 5.0 22.1 1.0 N1 B:IPU2830 5.0 24.3 1.0 CD1 B:TRP180 5.0 23.9 1.0

H.Li, C.S.Raman, P.Martasek, V.Kral, B.S.Masters, T.L.Poulos. Mapping the Active Site Polarity in Structures of Endothelial Nitric Oxide Synthase Heme Domain Complexed with Isothioureas. J.Inorg.Biochem. V. 81 133 2000.
ISSN: ISSN 0162-0134
PubMed: 11051558
DOI: 10.1016/S0162-0134(00)00099-4