Iron in PDB 3nos: Human Endothelial Nitric Oxide Synthase with Arginine Substrate

All present enzymatic activity of Human Endothelial Nitric Oxide Synthase with Arginine Substrate:
1.14.13.39;

The structure of Human Endothelial Nitric Oxide Synthase with Arginine Substrate, PDB code: 3nos was solved by T.O.Fischmann, P.C.Weber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.859, 93.264, 156.117, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 30.8

The structure of Human Endothelial Nitric Oxide Synthase with Arginine Substrate also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Iron atom in the Human Endothelial Nitric Oxide Synthase with Arginine Substrate (pdb code 3nos). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Human Endothelial Nitric Oxide Synthase with Arginine Substrate, PDB code: 3nos:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Human Endothelial Nitric Oxide Synthase with Arginine Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Endothelial Nitric Oxide Synthase with Arginine Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe510 b:16.3 occ:1.00 FE A:HEM510 0.0 16.3 1.0 ND A:HEM510 2.0 20.0 1.0 NA A:HEM510 2.1 27.0 1.0 NC A:HEM510 2.2 29.8 1.0 NB A:HEM510 2.2 17.9 1.0 SG A:CYS184 2.3 16.6 1.0 C4D A:HEM510 2.9 22.4 1.0 C1A A:HEM510 3.0 23.6 1.0 C1D A:HEM510 3.1 23.2 1.0 C4A A:HEM510 3.1 22.3 1.0 C1B A:HEM510 3.2 25.3 1.0 CB A:CYS184 3.2 14.0 1.0 C1C A:HEM510 3.2 27.8 1.0 C4C A:HEM510 3.2 28.2 1.0 C4B A:HEM510 3.2 19.0 1.0 CHA A:HEM510 3.3 20.8 1.0 CHD A:HEM510 3.5 27.4 1.0 CHB A:HEM510 3.5 23.4 1.0 CHC A:HEM510 3.6 22.6 1.0 CA A:CYS184 4.0 11.2 1.0 C3D A:HEM510 4.1 21.3 1.0 C2D A:HEM510 4.2 22.6 1.0 C2A A:HEM510 4.3 26.3 1.0 C3A A:HEM510 4.3 22.6 1.0 NE1 A:TRP178 4.3 14.6 1.0 CZ A:HAR512 4.4 49.0 1.0 C2B A:HEM510 4.4 21.1 1.0 C3B A:HEM510 4.4 19.1 1.0 NH1 A:HAR512 4.4 49.3 1.0 C3C A:HEM510 4.4 26.6 1.0 C2C A:HEM510 4.5 31.1 1.0 NH2 A:HAR512 4.5 49.5 1.0 OH1 A:HAR512 4.6 40.0 1.0 N A:GLY186 4.6 19.7 1.0 C A:CYS184 4.7 11.8 1.0 N A:VAL185 4.8 11.1 1.0 NE A:HAR512 4.8 45.9 1.0 CD1 A:TRP178 5.0 13.8 1.0

Iron binding site 2 out of 2 in the Human Endothelial Nitric Oxide Synthase with Arginine Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Endothelial Nitric Oxide Synthase with Arginine Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1010 b:26.1 occ:1.00 FE B:HEM1010 0.0 26.1 1.0 ND B:HEM1010 2.1 26.6 1.0 NB B:HEM1010 2.1 24.5 1.0 NC B:HEM1010 2.2 30.4 1.0 NA B:HEM1010 2.2 27.5 1.0 SG B:CYS184 2.3 19.8 1.0 C1B B:HEM1010 3.1 27.9 1.0 C4D B:HEM1010 3.1 28.2 1.0 C4B B:HEM1010 3.1 23.0 1.0 C1D B:HEM1010 3.1 29.7 1.0 C1C B:HEM1010 3.1 27.5 1.0 C1A B:HEM1010 3.2 27.8 1.0 C4C B:HEM1010 3.2 29.8 1.0 C4A B:HEM1010 3.2 25.1 1.0 CB B:CYS184 3.3 16.1 1.0 CHA B:HEM1010 3.5 26.0 1.0 CHB B:HEM1010 3.5 24.7 1.0 CHD B:HEM1010 3.5 28.7 1.0 CHC B:HEM1010 3.5 23.7 1.0 CA B:CYS184 4.1 11.7 1.0 C2B B:HEM1010 4.3 22.2 1.0 C3B B:HEM1010 4.3 21.6 1.0 C3D B:HEM1010 4.3 29.6 1.0 C2D B:HEM1010 4.3 27.2 1.0 NE1 B:TRP178 4.3 15.1 1.0 C3C B:HEM1010 4.4 33.0 1.0 C2A B:HEM1010 4.4 27.5 1.0 C2C B:HEM1010 4.4 30.4 1.0 C3A B:HEM1010 4.4 25.7 1.0 CZ B:HAR1012 4.6 52.5 1.0 NH2 B:HAR1012 4.6 50.3 1.0 N B:GLY186 4.7 18.6 1.0 NH1 B:HAR1012 4.7 52.6 1.0 C B:CYS184 4.8 11.0 1.0 N B:VAL185 4.9 12.4 1.0 CD1 B:TRP178 4.9 13.5 1.0 OH1 B:HAR1012 4.9 50.4 1.0

T.O.Fischmann, A.Hruza, X.D.Niu, J.D.Fossetta, C.A.Lunn, E.Dolphin, A.J.Prongay, P.Reichert, D.J.Lundell, S.K.Narula, P.C.Weber. Structural Characterization of Nitric Oxide Synthase Isoforms Reveals Striking Active-Site Conservation. Nat.Struct.Biol. V. 6 233 1999.
ISSN: ISSN 1072-8368
PubMed: 10074942
DOI: 10.1038/6675