Gadolinium in PDB 8ufs: Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride

The structure of Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride, PDB code: 8ufs was solved by H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.10 / 2.05
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.821, 152.24, 108.492, 90, 90.78, 90
R / Rfree (%)	18.5 / 23.5

The structure of Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride also contains other interesting chemical elements:

Iron	(Fe)	4 atoms
Chlorine	(Cl)	4 atoms
Zinc	(Zn)	2 atoms
Calcium	(Ca)	1 atom

The binding sites of Gadolinium atom in the Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride (pdb code 8ufs). This binding sites where shown within 5.0 Angstroms radius around Gadolinium atom.
In total 4 binding sites of Gadolinium where determined in the Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride, PDB code: 8ufs:
Jump to Gadolinium binding site number: 1; 2; 3; 4;

Gadolinium binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


Mono view


Stereo pair view

A full contact list of Gadolinium with other atoms in the Gd binding site number 1 of Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range: probe atom residue distance (Å) B Occ A:Gd509 b:61.3 occ:0.71 O3 A:BTB503 2.6 20.6 1.0 N A:BTB503 2.6 73.7 1.0 O4 A:BTB503 2.7 68.5 1.0 O6 A:BTB503 2.7 84.0 1.0 O A:HOH609 2.8 45.6 1.0 O8 A:BTB503 2.8 74.1 1.0 O A:HOH688 2.8 66.0 1.0 C2 A:BTB503 3.0 66.8 1.0 C4 A:BTB503 3.0 67.3 1.0 C3 A:BTB503 3.1 43.3 1.0 C5 A:BTB503 3.4 77.3 1.0 C6 A:BTB503 3.4 81.9 1.0 C7 A:BTB503 3.7 72.5 1.0 C8 A:BTB503 3.7 69.0 1.0 C1 A:BTB503 4.4 77.8 1.0 OD2 A:ASP384 4.6 48.0 1.0 OD1 A:ASP384 4.7 42.7 1.0

Gadolinium binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


Mono view


Stereo pair view

A full contact list of Gadolinium with other atoms in the Gd binding site number 2 of Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range: probe atom residue distance (Å) B Occ B:Gd508 b:34.5 occ:1.00 O B:HOH738 2.5 40.1 1.0 O4 B:BTB503 2.6 42.2 1.0 O B:THR319 2.6 25.9 1.0 O C:HOH613 2.7 32.8 1.0 OE1 B:GLU321 2.7 40.5 1.0 O8 B:BTB503 2.7 48.2 1.0 O3 B:BTB503 2.7 55.1 1.0 N B:BTB503 2.8 35.8 1.0 C6 B:BTB503 2.8 41.5 1.0 O6 B:BTB503 2.8 54.1 1.0 C8 B:BTB503 3.2 46.0 1.0 C5 B:BTB503 3.3 27.5 1.0 C2 B:BTB503 3.5 51.3 1.0 C3 B:BTB503 3.5 54.5 1.0 C7 B:BTB503 3.5 45.0 1.0 CD B:GLU321 3.6 42.9 1.0 C4 B:BTB503 3.6 53.3 1.0 C B:THR319 3.7 42.2 1.0 OE2 B:GLU321 3.7 43.1 1.0 CA B:THR319 4.4 38.6 1.0 OD1 C:ASP378 4.5 45.0 1.0 CB B:THR319 4.6 34.6 1.0 N B:GLU321 4.6 33.0 1.0 CA B:LEU320 4.6 32.0 1.0 N B:LEU320 4.6 34.6 1.0 OD2 C:ASP378 4.6 40.4 1.0 C1 B:BTB503 4.9 57.0 1.0 CG B:GLU321 5.0 40.0 1.0

Gadolinium binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


Mono view


Stereo pair view

A full contact list of Gadolinium with other atoms in the Gd binding site number 3 of Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range: probe atom residue distance (Å) B Occ B:Gd511 b:57.4 occ:0.72 O3 B:BTB509 2.4 7.4 1.0 O B:HOH602 2.6 37.2 1.0 O4 B:BTB509 2.7 76.4 1.0 O B:HOH733 2.7 49.4 1.0 O6 B:BTB509 2.7 73.4 1.0 O8 B:BTB509 2.8 61.6 1.0 N B:BTB509 2.8 67.8 1.0 C3 B:BTB509 3.3 33.8 1.0 O B:HOH809 3.3 51.0 1.0 C2 B:BTB509 3.3 61.5 1.0 C8 B:BTB509 3.3 61.9 1.0 C4 B:BTB509 3.4 70.9 1.0 C7 B:BTB509 3.6 66.0 1.0 C5 B:BTB509 3.7 68.8 1.0 C6 B:BTB509 3.7 72.0 1.0 OD2 B:ASP378 4.3 74.3 1.0 OD1 C:ASP384 4.3 69.6 1.0 OD1 B:ASP378 4.7 72.6 1.0 OD2 C:ASP384 4.7 70.6 1.0 C1 B:BTB509 4.8 63.1 1.0 CG B:ASP378 5.0 62.5 1.0 CG C:ASP384 5.0 61.1 1.0

Gadolinium binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


Mono view


Stereo pair view

A full contact list of Gadolinium with other atoms in the Gd binding site number 4 of Structure of Human Endothelial Nitric Oxide Synthase E361Q Mutant Heme Domain Obtain After Soaking Crystal with 4-Methyl-7-(4-Methyl-2,3,4, 5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range: probe atom residue distance (Å) B Occ D:Gd508 b:38.5 occ:1.00 O D:HOH782 2.5 34.8 1.0 O D:THR319 2.6 22.9 1.0 O4 D:BTB503 2.6 46.5 1.0 OE1 D:GLU321 2.7 53.4 1.0 O3 D:BTB503 2.7 61.0 1.0 O6 D:BTB503 2.7 26.3 1.0 O8 D:BTB503 2.8 49.0 1.0 N D:BTB503 2.8 64.3 1.0 C6 D:BTB503 2.8 30.3 1.0 C5 D:BTB503 3.4 43.1 1.0 C8 D:BTB503 3.4 54.6 1.0 C2 D:BTB503 3.5 74.3 1.0 C3 D:BTB503 3.5 71.4 1.0 C4 D:BTB503 3.5 65.2 1.0 CD D:GLU321 3.7 47.1 1.0 C7 D:BTB503 3.7 57.4 1.0 C D:THR319 3.8 49.8 1.0 OE2 D:GLU321 3.9 55.2 1.0 CA D:THR319 4.5 42.0 1.0 CB D:THR319 4.6 40.6 1.0 N D:GLU321 4.7 32.6 1.0 N D:LEU320 4.7 36.9 1.0 CA D:LEU320 4.7 38.0 1.0 O D:HOH753 4.7 35.5 1.0 C1 D:BTB503 4.9 77.7 1.0

H.Li, C.D.Hardy, C.T.Reidl, Q.Jing, F.Xue, M.Cinelli, R.B.Silverman, T.L.Poulos. Crystallographic and Computational Insights Into Isoform-Selective Dynamics in Nitric Oxide Synthase. Biochemistry 2024.
ISSN: ISSN 0006-2960
PubMed: 38417024
DOI: 10.1021/ACS.BIOCHEM.3C00601