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Iron in PDB 4uqr: Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with N-Omega-Nitro-L-Arginine

Enzymatic activity of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with N-Omega-Nitro-L-Arginine

All present enzymatic activity of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with N-Omega-Nitro-L-Arginine:
1.14.13.165;

Protein crystallography data

The structure of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with N-Omega-Nitro-L-Arginine, PDB code: 4uqr was solved by J.K.Holden, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.72
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 80.606, 94.820, 62.892, 90.00, 90.00, 90.00
R / Rfree (%) 16.805 / 19.912

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with N-Omega-Nitro-L-Arginine (pdb code 4uqr). 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 Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with N-Omega-Nitro-L-Arginine, PDB code: 4uqr:

Iron binding site 1 out of 1 in 4uqr

Go back to Iron Binding Sites List in 4uqr
Iron binding site 1 out of 1 in the Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with N-Omega-Nitro-L-Arginine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with N-Omega-Nitro-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe901

b:18.4
occ:1.00
 FE A:HEM901 0.0 18.4 1.0
ND A:HEM901 1.9 19.1 1.0
NA A:HEM901 2.0 18.4 1.0
NB A:HEM901 2.1 19.0 1.0
NC A:HEM901 2.1 20.7 1.0
SG A:CYS66 2.5 19.1 1.0
C1D A:HEM901 3.0 18.2 1.0
C4D A:HEM901 3.0 17.3 1.0
C1A A:HEM901 3.0 19.4 1.0
C4A A:HEM901 3.0 17.3 1.0
C4B A:HEM901 3.0 18.4 1.0
C1B A:HEM901 3.1 17.9 1.0
C4C A:HEM901 3.1 18.8 1.0
C1C A:HEM901 3.1 19.6 1.0
CB A:CYS66 3.4 18.9 1.0
CHA A:HEM901 3.4 18.8 1.0
CHC A:HEM901 3.4 18.5 1.0
CHD A:HEM901 3.4 17.9 1.0
CHB A:HEM901 3.4 18.6 1.0
NH1 A:NRG904 4.0 21.8 1.0
CA A:CYS66 4.2 18.9 1.0
C3A A:HEM901 4.2 18.0 1.0
C2A A:HEM901 4.2 18.2 1.0
C2D A:HEM901 4.2 18.7 1.0
N1 A:NRG904 4.2 23.0 1.0
CZ A:NRG904 4.3 20.1 1.0
C3D A:HEM901 4.3 18.4 1.0
C2B A:HEM901 4.3 17.6 1.0
C2C A:HEM901 4.3 18.6 1.0
C3C A:HEM901 4.3 18.9 1.0
C3B A:HEM901 4.3 18.5 1.0
NE1 A:TRP60 4.4 18.2 1.0
O3 A:NRG904 4.4 22.4 1.0
NH2 A:NRG904 4.6 16.6 1.0
O2 A:NRG904 4.7 23.9 1.0
NE A:NRG904 4.8 18.7 1.0
N A:GLY68 4.9 17.9 1.0
C A:CYS66 5.0 19.7 1.0

Reference:

J.K.Holden, N.Lim, T.L.Poulos. Identification of Redox Partners and Development of A Novel Chimeric Bacterial Nitric Oxide Synthase For Structure Activity Analyses. J.Biol.Chem. V. 289 29437 2014.
ISSN: ISSN 0021-9258
PubMed: 25194416
DOI: 10.1074/JBC.M114.595165
Page generated: Mon Aug 5 13:35:44 2024

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