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Iron in PDB 2nos: Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114), Aminoguanidine Complex

Enzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114), Aminoguanidine Complex

All present enzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114), Aminoguanidine Complex:
1.14.13.39;

Protein crystallography data

The structure of Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114), Aminoguanidine Complex, PDB code: 2nos was solved by B.R.Crane, A.S.Arvai, E.D.Getzoff, D.J.Stuehr, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.000, 73.800, 92.800, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 26.7

Iron Binding Sites:

The binding sites of Iron atom in the Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114), Aminoguanidine Complex (pdb code 2nos). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114), Aminoguanidine Complex, PDB code: 2nos:

Iron binding site 1 out of 1 in 2nos

Go back to Iron Binding Sites List in 2nos
Iron binding site 1 out of 1 in the Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114), Aminoguanidine Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114), Aminoguanidine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe901

b:17.7
occ:1.00
 FE A:HEM901 0.0 17.7 1.0
ND A:HEM901 1.9 19.6 1.0
NC A:HEM901 1.9 17.6 1.0
NB A:HEM901 1.9 17.9 1.0
NA A:HEM901 2.0 21.7 1.0
N1 A:IMD902 2.0 29.9 1.0
SG A:CYS194 2.3 18.5 1.0
C1C A:HEM901 3.0 15.5 1.0
C4D A:HEM901 3.0 20.3 1.0
C5 A:IMD902 3.0 32.1 1.0
C4B A:HEM901 3.0 15.1 1.0
C1D A:HEM901 3.0 18.8 1.0
C1B A:HEM901 3.0 18.4 1.0
C4C A:HEM901 3.0 17.0 1.0
C4A A:HEM901 3.0 21.1 1.0
C1A A:HEM901 3.0 22.2 1.0
C2 A:IMD902 3.0 36.4 1.0
CHC A:HEM901 3.3 17.7 1.0
CHA A:HEM901 3.4 16.9 1.0
CHD A:HEM901 3.4 14.8 1.0
CHB A:HEM901 3.4 21.4 1.0
CB A:CYS194 3.5 19.5 1.0
C4 A:IMD902 4.1 29.7 1.0
N3 A:IMD902 4.1 35.5 1.0
CA A:CYS194 4.2 20.9 1.0
C3D A:HEM901 4.2 23.0 1.0
C2D A:HEM901 4.2 15.6 1.0
C2C A:HEM901 4.2 18.3 1.0
C2B A:HEM901 4.2 19.9 1.0
C3B A:HEM901 4.2 16.7 1.0
C3C A:HEM901 4.2 14.8 1.0
C3A A:HEM901 4.3 20.7 1.0
C2A A:HEM901 4.3 23.3 1.0
NE1 A:TRP188 4.4 12.0 1.0
N1 A:AGU903 4.7 50.0 1.0
N A:GLY196 4.9 27.3 1.0
C A:CYS194 4.9 23.2 1.0

Reference:

B.R.Crane, A.S.Arvai, R.Gachhui, C.Wu, D.K.Ghosh, E.D.Getzoff, D.J.Stuehr, J.A.Tainer. The Structure of Nitric Oxide Synthase Oxygenase Domain and Inhibitor Complexes. Science V. 278 425 1997.
ISSN: ISSN 0036-8075
PubMed: 9334294
DOI: 10.1126/SCIENCE.278.5337.425
Page generated: Thu Jul 17 03:02:26 2025

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