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Iron in PDB 5g65: Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Quinolin-2-Amine

Enzymatic activity of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Quinolin-2-Amine

All present enzymatic activity of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Quinolin-2-Amine:
1.14.13.165;

Protein crystallography data

The structure of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Quinolin-2-Amine, PDB code: 5g65 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) 34.13 / 2.03
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 80.560, 94.800, 62.070, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 22.3

Other elements in 5g65:

The structure of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Quinolin-2-Amine also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Quinolin-2-Amine (pdb code 5g65). 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 Quinolin-2-Amine, PDB code: 5g65:

Iron binding site 1 out of 1 in 5g65

Go back to Iron Binding Sites List in 5g65
Iron binding site 1 out of 1 in the Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Quinolin-2-Amine


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 Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1364

b:18.7
occ:1.00
 FE A:HEM1364 0.0 18.7 1.0
ND A:HEM1364 1.9 16.2 1.0
NA A:HEM1364 2.0 12.9 1.0
NC A:HEM1364 2.1 17.3 1.0
NB A:HEM1364 2.1 15.4 1.0
SG A:CYS66 2.7 19.8 1.0
C1D A:HEM1364 2.9 16.6 1.0
C4D A:HEM1364 2.9 19.2 1.0
C1A A:HEM1364 3.0 18.1 1.0
C4C A:HEM1364 3.0 18.7 1.0
C4A A:HEM1364 3.1 16.2 1.0
C4B A:HEM1364 3.1 17.0 1.0
C1B A:HEM1364 3.1 15.7 1.0
C1C A:HEM1364 3.1 18.2 1.0
CHD A:HEM1364 3.3 17.7 1.0
CB A:CYS66 3.4 12.0 1.0
CHA A:HEM1364 3.4 20.5 1.0
CHC A:HEM1364 3.5 16.0 1.0
C4 A:2AQ1366 3.5 16.7 1.0
CHB A:HEM1364 3.5 14.6 1.0
C5 A:2AQ1366 3.6 19.2 1.0
C6 A:2AQ1366 3.8 20.9 1.0
C3 A:2AQ1366 4.0 18.1 1.0
C10 A:2AQ1366 4.1 19.1 1.0
C2D A:HEM1364 4.1 14.9 1.0
CA A:CYS66 4.1 13.0 1.0
C3D A:HEM1364 4.1 18.2 1.0
C2A A:HEM1364 4.2 16.5 1.0
C3A A:HEM1364 4.2 19.9 1.0
C3C A:HEM1364 4.3 20.3 1.0
C2C A:HEM1364 4.3 20.6 1.0
C2B A:HEM1364 4.3 17.2 1.0
C3B A:HEM1364 4.4 18.7 1.0
NE1 A:TRP60 4.5 21.5 1.0
C2 A:2AQ1366 4.5 17.6 1.0
C7 A:2AQ1366 4.6 20.1 1.0
N11 A:2AQ1366 4.6 15.6 1.0
C9 A:2AQ1366 4.8 16.6 1.0
C A:CYS66 4.9 15.2 1.0

Reference:

J.K.Holden, M.C.Lewis, M.A.Cinelli, Z.Abdullatif, A.V.Pensa, R.B.Silverman, T.L.Poulos. Targeting Bacterial Nitric Oxide Synthase with Aminoquinoline-Based Inhibitors. Biochemistry V. 55 5587 2016.
ISSN: ISSN 1520-4995
PubMed: 27607918
DOI: 10.1021/ACS.BIOCHEM.6B00786
Page generated: Tue Aug 6 01:26:15 2024

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