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Iron in PDB 1m9r: Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound

Enzymatic activity of Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound

All present enzymatic activity of Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound:
1.14.13.39;

Protein crystallography data

The structure of Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound, PDB code: 1m9r was solved by R.J.Rosenfeld, E.D.Garcin, K.Panda, G.Andersson, A.Aberg, A.V.Wallace, D.J.Stuehr, J.A.Tainer, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.65 / 2.56
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.625, 90.280, 155.490, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 26.6

Other elements in 1m9r:

The structure of Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound also contains other interesting chemical elements:

Bromine (Br) 4 atoms
Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound (pdb code 1m9r). 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 3-Bromo-7- Nitroindazole Bound, PDB code: 1m9r:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1m9r

Go back to Iron Binding Sites List in 1m9r
Iron binding site 1 out of 2 in the Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound


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 3-Bromo-7- Nitroindazole Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe901

b:36.7
occ:1.00
FE A:HEM901 0.0 36.7 1.0
NA A:HEM901 2.0 39.0 1.0
NC A:HEM901 2.1 37.6 1.0
ND A:HEM901 2.1 39.5 1.0
NB A:HEM901 2.1 39.2 1.0
SG A:CYS184 2.3 33.6 1.0
C4D A:HEM901 3.0 40.4 1.0
C1A A:HEM901 3.1 39.9 1.0
C4C A:HEM901 3.1 38.7 1.0
C1C A:HEM901 3.1 37.6 1.0
C1D A:HEM901 3.1 38.9 1.0
C4A A:HEM901 3.1 39.4 1.0
C4B A:HEM901 3.1 38.0 1.0
C1B A:HEM901 3.1 39.6 1.0
CB A:CYS184 3.2 34.6 1.0
CHA A:HEM901 3.4 39.9 1.0
CHD A:HEM901 3.4 40.9 1.0
CHC A:HEM901 3.4 37.6 1.0
CHB A:HEM901 3.5 39.3 1.0
CA A:CYS184 3.9 35.6 1.0
C9 A:INE906 4.0 44.8 1.0
C3 A:INE906 4.2 44.8 1.0
C4 A:INE906 4.2 45.0 1.0
C3D A:HEM901 4.2 40.7 1.0
C2D A:HEM901 4.3 38.9 1.0
NE1 A:TRP178 4.3 40.5 1.0
C2C A:HEM901 4.3 38.5 1.0
C3C A:HEM901 4.3 39.5 1.0
C3A A:HEM901 4.3 39.4 1.0
C2A A:HEM901 4.3 41.8 1.0
C3B A:HEM901 4.3 39.9 1.0
C2B A:HEM901 4.4 39.2 1.0
C8 A:INE906 4.4 44.0 1.0
N2 A:INE906 4.6 45.3 1.0
BR A:INE906 4.7 45.0 1.0
N1 A:INE906 4.7 44.2 1.0
C5 A:INE906 4.8 44.3 1.0
C A:CYS184 4.8 34.9 1.0
CD1 A:TRP178 4.9 39.2 1.0
N A:VAL185 4.9 34.4 1.0
C7 A:INE906 4.9 45.2 1.0

Iron binding site 2 out of 2 in 1m9r

Go back to Iron Binding Sites List in 1m9r
Iron binding site 2 out of 2 in the Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound


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 3-Bromo-7- Nitroindazole Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe901

b:31.9
occ:1.00
FE B:HEM901 0.0 31.9 1.0
ND B:HEM901 2.0 33.2 1.0
NB B:HEM901 2.1 32.6 1.0
NA B:HEM901 2.1 35.7 1.0
NC B:HEM901 2.1 33.8 1.0
SG B:CYS184 2.3 33.5 1.0
C1D B:HEM901 3.1 34.0 1.0
C4B B:HEM901 3.1 32.2 1.0
C1B B:HEM901 3.1 33.2 1.0
C4D B:HEM901 3.1 36.7 1.0
C4A B:HEM901 3.1 35.2 1.0
C1A B:HEM901 3.1 36.9 1.0
C4C B:HEM901 3.1 33.0 1.0
C1C B:HEM901 3.1 33.5 1.0
CB B:CYS184 3.2 31.3 1.0
CHB B:HEM901 3.4 33.5 1.0
CHD B:HEM901 3.4 35.1 1.0
CHA B:HEM901 3.4 35.7 1.0
CHC B:HEM901 3.4 33.5 1.0
CA B:CYS184 4.0 32.6 1.0
C9 B:INE907 4.1 44.4 1.0
C4 B:INE907 4.3 43.9 1.0
NE1 B:TRP178 4.3 31.5 1.0
C2D B:HEM901 4.3 35.9 1.0
C3B B:HEM901 4.3 31.3 1.0
C3A B:HEM901 4.3 38.4 1.0
C2B B:HEM901 4.3 32.4 1.0
C3 B:INE907 4.3 44.4 1.0
C3D B:HEM901 4.3 39.3 1.0
C2A B:HEM901 4.3 39.6 1.0
C3C B:HEM901 4.4 33.1 1.0
C2C B:HEM901 4.4 33.9 1.0
C8 B:INE907 4.5 43.7 1.0
C5 B:INE907 4.8 46.0 1.0
N2 B:INE907 4.8 42.9 1.0
C B:CYS184 4.8 32.6 1.0
N1 B:INE907 4.8 43.6 1.0
BR B:INE907 4.9 47.7 1.0
C7 B:INE907 4.9 44.6 1.0
N B:VAL185 4.9 32.6 1.0
N B:GLY186 4.9 33.5 1.0
CD1 B:TRP178 5.0 29.7 1.0

Reference:

R.J.Rosenfeld, E.D.Garcin, K.Panda, G.Andersson, A.Aberg, A.V.Wallace, G.M.Morris, A.J.Olson, D.J.Stuehr, J.A.Tainer, E.D.Getzoff. Conformational Changes in Nitric Oxide Synthases Induced By Chlorzoxazone and Nitroindazoles: Crystallographic and Computational Analyses of Inhibitor Potency Biochemistry V. 41 13915 2002.
ISSN: ISSN 0006-2960
PubMed: 12437348
DOI: 10.1021/BI026313J
Page generated: Sun Dec 13 14:23:26 2020

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