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Iron in PDB 4cum: Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One

Enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One

All present enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One:
1.14.13.39;

Protein crystallography data

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One, PDB code: 4cum was solved by G.Chreifi, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 88.04 / 2.33
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.011, 106.493, 156.480, 90.00, 90.00, 90.00
R / Rfree (%) 16.951 / 22.703

Other elements in 4cum:

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One also contains other interesting chemical elements:

Arsenic (As) 2 atoms
Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One (pdb code 4cum). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One, PDB code: 4cum:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 4cum

Go back to Iron Binding Sites List in 4cum
Iron binding site 1 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:35.2
occ:1.00
 FE A:HEM500 0.0 35.2 1.0
NC A:HEM500 1.9 31.0 1.0
NA A:HEM500 2.0 31.2 1.0
NB A:HEM500 2.1 29.6 1.0
ND A:HEM500 2.1 29.6 1.0
SG A:CYS186 2.4 39.2 1.0
C4C A:HEM500 3.0 32.1 1.0
C4A A:HEM500 3.1 31.0 1.0
C1D A:HEM500 3.1 32.5 1.0
C1B A:HEM500 3.1 29.6 1.0
C1C A:HEM500 3.1 29.8 1.0
C1A A:HEM500 3.1 32.4 1.0
C4B A:HEM500 3.1 33.3 1.0
C4D A:HEM500 3.2 32.6 1.0
CB A:CYS186 3.3 37.5 1.0
CHD A:HEM500 3.4 30.6 1.0
CHB A:HEM500 3.4 31.4 1.0
CHC A:HEM500 3.6 32.5 1.0
CHA A:HEM500 3.6 33.9 1.0
NH2 A:ARG700 4.0 42.9 1.0
CA A:CYS186 4.1 36.1 1.0
C3C A:HEM500 4.2 30.8 1.0
NE1 A:TRP180 4.3 35.7 1.0
C2C A:HEM500 4.3 30.3 1.0
C3A A:HEM500 4.3 29.5 1.0
C2A A:HEM500 4.4 34.4 1.0
C2B A:HEM500 4.4 31.6 1.0
C2D A:HEM500 4.4 35.2 1.0
C3B A:HEM500 4.4 32.8 1.0
CZ A:ARG700 4.5 41.3 1.0
C3D A:HEM500 4.5 35.0 1.0
N A:GLY188 4.8 38.0 1.0
C A:CYS186 4.8 39.0 1.0
NE A:ARG700 4.9 40.4 1.0
CD1 A:TRP180 4.9 32.9 1.0

Iron binding site 2 out of 2 in 4cum

Go back to Iron Binding Sites List in 4cum
Iron binding site 2 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (9AS)-2-Amino-9A-Methyl-6,7,8,9,9A, 10-Hexahydrobenzo[G]Pteridin-4(3H)-One within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:39.6
occ:1.00
 FE B:HEM500 0.0 39.6 1.0
NC B:HEM500 2.0 39.1 1.0
NA B:HEM500 2.0 38.5 1.0
NB B:HEM500 2.1 38.2 1.0
ND B:HEM500 2.1 38.1 1.0
SG B:CYS186 2.4 38.4 1.0
C4C B:HEM500 3.1 38.7 1.0
C4A B:HEM500 3.1 37.4 1.0
C1D B:HEM500 3.1 41.0 1.0
C1C B:HEM500 3.1 38.5 1.0
C1A B:HEM500 3.1 37.5 1.0
C1B B:HEM500 3.1 38.3 1.0
C4B B:HEM500 3.1 37.9 1.0
C4D B:HEM500 3.2 38.3 1.0
CHD B:HEM500 3.4 39.5 1.0
CHB B:HEM500 3.5 38.9 1.0
CB B:CYS186 3.5 37.7 1.0
CHC B:HEM500 3.5 37.2 1.0
CHA B:HEM500 3.6 35.7 1.0
NH2 B:ARG700 3.9 47.1 1.0
CA B:CYS186 4.2 34.3 1.0
NE1 B:TRP180 4.3 39.8 1.0
C3C B:HEM500 4.3 37.5 1.0
C3A B:HEM500 4.4 37.8 1.0
CZ B:ARG700 4.4 44.6 1.0
C2C B:HEM500 4.4 38.9 1.0
C2A B:HEM500 4.4 40.1 1.0
C3B B:HEM500 4.5 37.6 1.0
C2D B:HEM500 4.5 40.0 1.0
C2B B:HEM500 4.5 38.2 1.0
C3D B:HEM500 4.5 38.2 1.0
NH1 B:ARG700 4.8 42.9 1.0
N B:GLY188 4.8 36.6 1.0
N B:VAL187 4.9 33.3 1.0
C B:CYS186 4.9 33.3 1.0
NE B:ARG700 4.9 42.0 1.0
CD1 B:TRP180 4.9 35.6 1.0

Reference:

G.Chreifi, H.Li, C.R.Mcinnes, C.L.Gibson, C.J.Suckling, T.L.Poulos. Communication Between the Zinc and Tetrahydrobiopterin Binding Sites in Nitric Oxide Synthase. Biochemistry V. 53 4216 2014.
ISSN: ISSN 0006-2960
PubMed: 24819538
DOI: 10.1021/BI5003986
Page generated: Mon Aug 5 00:43:06 2024

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