Iron in PDB 1ed5: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with Nna(H4B Free)

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

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with Nna(H4B Free), PDB code: 1ed5 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)	39.46 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.826, 106.417, 156.163, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 23.8

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with Nna(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 Nna(H4B Free) (pdb code 1ed5). 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 Nna(H4B Free), PDB code: 1ed5:
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 Nna(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 Nna(H4B Free) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1500 b:22.6 occ:1.00 FE A:HEM1500 0.0 22.6 1.0 NA A:HEM1500 2.0 23.9 1.0 NB A:HEM1500 2.0 19.9 1.0 NC A:HEM1500 2.0 22.5 1.0 ND A:HEM1500 2.0 17.1 1.0 SG A:CYS186 2.3 23.0 1.0 C1A A:HEM1500 3.1 20.5 1.0 C1B A:HEM1500 3.1 23.9 1.0 C4A A:HEM1500 3.1 20.4 1.0 C4B A:HEM1500 3.1 21.6 1.0 C4D A:HEM1500 3.1 19.9 1.0 C1D A:HEM1500 3.1 22.8 1.0 C1C A:HEM1500 3.1 20.0 1.0 C4C A:HEM1500 3.1 22.0 1.0 CB A:CYS186 3.4 24.0 1.0 CHB A:HEM1500 3.5 22.1 1.0 CHA A:HEM1500 3.5 21.6 1.0 CHD A:HEM1500 3.5 19.5 1.0 CHC A:HEM1500 3.5 22.3 1.0 NH1 A:NRG1705 4.0 27.2 1.0 CA A:CYS186 4.1 23.4 1.0 C2B A:HEM1500 4.3 20.2 1.0 C2A A:HEM1500 4.3 22.6 1.0 CZ A:NRG1705 4.3 30.0 1.0 C3A A:HEM1500 4.3 22.8 1.0 C2D A:HEM1500 4.3 19.6 1.0 C3B A:HEM1500 4.3 23.2 1.0 C2C A:HEM1500 4.3 22.2 1.0 C3D A:HEM1500 4.3 20.4 1.0 C3C A:HEM1500 4.4 21.9 1.0 NE1 A:TRP180 4.4 21.7 1.0 N1 A:NRG1705 4.4 30.1 1.0 NH2 A:NRG1705 4.7 21.7 1.0 NE A:NRG1705 4.7 26.4 1.0 O3 A:NRG1705 4.8 24.8 1.0 C A:CYS186 4.9 24.3 1.0 O2 A:NRG1705 4.9 25.3 1.0 N A:GLY188 4.9 23.6 1.0 N A:VAL187 4.9 24.2 1.0 CD A:NRG1705 5.0 26.8 1.0 CD1 A:TRP180 5.0 23.1 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with Nna(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 Nna(H4B Free) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2500 b:24.1 occ:1.00 FE B:HEM2500 0.0 24.1 1.0 ND B:HEM2500 2.0 26.1 1.0 NB B:HEM2500 2.0 24.0 1.0 NA B:HEM2500 2.0 25.0 1.0 NC B:HEM2500 2.0 25.5 1.0 SG B:CYS186 2.3 21.8 1.0 C4D B:HEM2500 3.1 24.7 1.0 C1D B:HEM2500 3.1 24.2 1.0 C1B B:HEM2500 3.1 22.3 1.0 C4A B:HEM2500 3.1 17.8 1.0 C4B B:HEM2500 3.1 26.8 1.0 C1A B:HEM2500 3.1 21.9 1.0 C1C B:HEM2500 3.1 25.9 1.0 C4C B:HEM2500 3.1 18.3 1.0 CB B:CYS186 3.4 24.9 1.0 CHB B:HEM2500 3.4 21.2 1.0 CHD B:HEM2500 3.4 21.6 1.0 CHC B:HEM2500 3.5 26.0 1.0 CHA B:HEM2500 3.5 25.5 1.0 NH1 B:NRG2705 4.0 30.1 1.0 CA B:CYS186 4.1 24.4 1.0 C3D B:HEM2500 4.3 24.9 1.0 C2D B:HEM2500 4.3 25.4 1.0 C2B B:HEM2500 4.3 25.4 1.0 C3A B:HEM2500 4.3 21.5 1.0 C3B B:HEM2500 4.3 27.0 1.0 C2A B:HEM2500 4.3 23.9 1.0 N1 B:NRG2705 4.3 24.9 1.0 C2C B:HEM2500 4.4 24.0 1.0 C3C B:HEM2500 4.4 23.9 1.0 NE1 B:TRP180 4.4 28.2 1.0 CZ B:NRG2705 4.4 28.6 1.0 O3 B:NRG2705 4.7 28.0 1.0 O2 B:NRG2705 4.8 28.7 1.0 NH2 B:NRG2705 4.8 22.6 1.0 N B:GLY188 4.9 22.6 1.0 C B:CYS186 4.9 21.7 1.0 N B:VAL187 5.0 20.9 1.0

C.S.Raman, H.Li, P.Martasek, G.Southan, B.S.Masters, T.L.Poulos. Crystal Structure of Nitric Oxide Synthase Bound to Nitro Indazole Reveals A Novel Inactivation Mechanism. Biochemistry V. 40 13448 2001.
ISSN: ISSN 0006-2960
PubMed: 11695891
DOI: 10.1021/BI010957U