Iron in PDB 4nse: Bovine Endothelial Nitric Oxide Synthase, H4B-Free, L-Arg Complex

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase, H4B-Free, L-Arg Complex:
1.14.13.39;

The structure of Bovine Endothelial Nitric Oxide Synthase, H4B-Free, L-Arg Complex, PDB code: 4nse 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)	30.00 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.660, 106.100, 155.750, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 26

The structure of Bovine Endothelial Nitric Oxide Synthase, H4B-Free, L-Arg Complex 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, H4B-Free, L-Arg Complex (pdb code 4nse). 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, H4B-Free, L-Arg Complex, PDB code: 4nse:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Bovine Endothelial Nitric Oxide Synthase, H4B-Free, L-Arg Complex


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, H4B-Free, L-Arg Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:17.9 occ:1.00 FE A:HEM500 0.0 17.9 1.0 NB A:HEM500 1.9 14.7 1.0 ND A:HEM500 1.9 12.6 1.0 NC A:HEM500 2.0 19.4 1.0 NA A:HEM500 2.0 19.5 1.0 SG A:CYS186 2.3 28.6 1.0 C1B A:HEM500 3.0 18.1 1.0 C4B A:HEM500 3.0 20.5 1.0 C1D A:HEM500 3.0 22.3 1.0 C4D A:HEM500 3.0 21.2 1.0 C4A A:HEM500 3.1 16.9 1.0 C1C A:HEM500 3.1 18.8 1.0 C4C A:HEM500 3.1 20.2 1.0 C1A A:HEM500 3.1 16.1 1.0 CB A:CYS186 3.3 24.9 1.0 CHC A:HEM500 3.4 19.4 1.0 CHD A:HEM500 3.4 20.7 1.0 CHB A:HEM500 3.4 19.4 1.0 CHA A:HEM500 3.5 14.3 1.0 CA A:CYS186 4.0 20.5 1.0 C2B A:HEM500 4.2 16.9 1.0 C2D A:HEM500 4.2 19.3 1.0 C3B A:HEM500 4.2 20.2 1.0 C3D A:HEM500 4.2 23.6 1.0 C3A A:HEM500 4.3 18.7 1.0 C2A A:HEM500 4.3 19.7 1.0 NH1 A:ARG700 4.4 28.5 1.0 C2C A:HEM500 4.4 19.0 1.0 NE1 A:TRP180 4.4 17.1 1.0 C3C A:HEM500 4.4 19.2 1.0 CZ A:ARG700 4.5 28.5 1.0 NE A:ARG700 4.8 30.6 1.0 C A:CYS186 4.8 21.8 1.0 N A:GLY188 4.8 26.3 1.0 N A:VAL187 4.9 19.2 1.0 NH2 A:ARG700 4.9 26.4 1.0 CD A:ARG700 5.0 30.9 1.0

Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase, H4B-Free, L-Arg Complex


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, H4B-Free, L-Arg Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:37.2 occ:1.00 FE B:HEM500 0.0 37.2 1.0 ND B:HEM500 2.0 30.4 1.0 NB B:HEM500 2.0 30.5 1.0 NC B:HEM500 2.0 29.8 1.0 NA B:HEM500 2.0 33.0 1.0 SG B:CYS186 2.2 39.0 1.0 C1D B:HEM500 3.0 33.5 1.0 C4D B:HEM500 3.0 32.1 1.0 C4B B:HEM500 3.0 32.4 1.0 C1A B:HEM500 3.0 30.4 1.0 C1B B:HEM500 3.0 30.4 1.0 C1C B:HEM500 3.0 30.2 1.0 C4C B:HEM500 3.1 30.9 1.0 C4A B:HEM500 3.1 28.8 1.0 CHA B:HEM500 3.4 31.9 1.0 CHC B:HEM500 3.4 30.5 1.0 CHD B:HEM500 3.4 31.7 1.0 CHB B:HEM500 3.4 29.0 1.0 CB B:CYS186 3.5 29.3 1.0 NH1 B:ARG700 3.8 40.2 1.0 CA B:CYS186 4.2 26.8 1.0 C2D B:HEM500 4.2 34.1 1.0 C3D B:HEM500 4.3 33.4 1.0 C2B B:HEM500 4.3 30.3 1.0 CZ B:ARG700 4.3 42.2 1.0 C3B B:HEM500 4.3 32.8 1.0 NE1 B:TRP180 4.3 34.0 1.0 C2A B:HEM500 4.3 33.2 1.0 C2C B:HEM500 4.3 33.2 1.0 C3C B:HEM500 4.3 34.0 1.0 C3A B:HEM500 4.3 30.4 1.0 NH2 B:ARG700 4.7 37.0 1.0 N B:GLY188 4.8 26.1 1.0 NE B:ARG700 4.8 38.7 1.0 N B:VAL187 4.9 22.7 1.0 C B:CYS186 4.9 23.4 1.0

C.S.Raman, H.Li, P.Martasek, V.Kral, B.S.Masters, T.L.Poulos. Crystal Structure of Constitutive Endothelial Nitric Oxide Synthase: A Paradigm For Pterin Function Involving A Novel Metal Center. Cell(Cambridge,Mass.) V. 95 939 1998.
ISSN: ISSN 0092-8674
PubMed: 9875848
DOI: 10.1016/S0092-8674(00)81718-3