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Iron in PDB 1foo: Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free)

Enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free)

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free):
1.14.13.39;

Protein crystallography data

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free), PDB code: 1foo was solved by C.S.Raman, H.Li, P.Martasek, B.S.S.Masters, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.52 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.206, 106.555, 156.671, 90.00, 90.00, 90.00
R / Rfree (%) 22.3 / 25.3

Other elements in 1foo:

The structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free) 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 Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free) (pdb code 1foo). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free), PDB code: 1foo:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1foo

Go back to Iron Binding Sites List in 1foo
Iron binding site 1 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:28.9
occ:1.00
FE A:HEM500 0.0 28.9 1.0
N A:NO1910 1.8 31.5 1.0
NA A:HEM500 2.0 30.0 1.0
NC A:HEM500 2.0 28.7 1.0
NB A:HEM500 2.0 28.8 1.0
ND A:HEM500 2.0 29.5 1.0
SG A:CYS186 2.3 28.2 1.0
O A:NO1910 2.9 34.5 1.0
C1B A:HEM500 3.0 28.9 1.0
C1A A:HEM500 3.0 30.8 1.0
C1D A:HEM500 3.0 30.0 1.0
C4A A:HEM500 3.0 30.3 1.0
C4D A:HEM500 3.0 30.4 1.0
C4C A:HEM500 3.0 28.6 1.0
C4B A:HEM500 3.1 29.1 1.0
C1C A:HEM500 3.1 28.6 1.0
CB A:CYS186 3.4 28.1 1.0
CHD A:HEM500 3.4 29.0 1.0
CHB A:HEM500 3.4 29.2 1.0
CHA A:HEM500 3.4 29.9 1.0
CHC A:HEM500 3.5 28.9 1.0
CA A:CYS186 4.1 27.5 1.0
NH1 A:ARG1700 4.3 48.0 1.0
C2B A:HEM500 4.3 29.1 1.0
C2A A:HEM500 4.3 31.6 1.0
C3A A:HEM500 4.3 30.9 1.0
C3D A:HEM500 4.3 31.1 1.0
C2D A:HEM500 4.3 30.5 1.0
C2C A:HEM500 4.3 27.5 1.0
C3B A:HEM500 4.3 29.0 1.0
C3C A:HEM500 4.3 27.6 1.0
NE1 A:TRP180 4.5 26.0 1.0
CZ A:ARG1700 4.7 47.6 1.0
CD A:ARG1700 4.9 46.8 1.0
C A:CYS186 4.9 27.4 1.0
NE A:ARG1700 5.0 47.3 1.0
N A:GLY188 5.0 26.9 1.0

Iron binding site 2 out of 2 in 1foo

Go back to Iron Binding Sites List in 1foo
Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L- Arg and No(H4B-Free) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:31.6
occ:1.00
FE B:HEM500 0.0 31.6 1.0
N B:NO2910 1.8 33.1 1.0
NB B:HEM500 2.0 31.6 1.0
NC B:HEM500 2.0 31.5 1.0
ND B:HEM500 2.0 31.9 1.0
NA B:HEM500 2.0 31.7 1.0
SG B:CYS186 2.3 30.9 1.0
O B:NO2910 2.9 35.1 1.0
C1C B:HEM500 3.0 31.5 1.0
C1B B:HEM500 3.0 31.6 1.0
C4C B:HEM500 3.0 31.2 1.0
C4B B:HEM500 3.0 32.1 1.0
C1D B:HEM500 3.0 31.6 1.0
C4D B:HEM500 3.1 32.1 1.0
C4A B:HEM500 3.1 31.1 1.0
C1A B:HEM500 3.1 31.7 1.0
CB B:CYS186 3.4 29.7 1.0
CHC B:HEM500 3.4 31.8 1.0
CHD B:HEM500 3.4 31.5 1.0
CHB B:HEM500 3.4 31.2 1.0
CHA B:HEM500 3.5 31.8 1.0
CA B:CYS186 4.1 29.5 1.0
C2B B:HEM500 4.3 31.8 1.0
C2C B:HEM500 4.3 31.5 1.0
C2D B:HEM500 4.3 32.4 1.0
C3D B:HEM500 4.3 32.8 1.0
C3C B:HEM500 4.3 31.9 1.0
NH1 B:ARG2700 4.3 48.6 1.0
C3B B:HEM500 4.3 31.9 1.0
C3A B:HEM500 4.3 31.4 1.0
C2A B:HEM500 4.3 32.3 1.0
NE1 B:TRP180 4.4 28.3 1.0
CZ B:ARG2700 4.7 47.8 1.0
C B:CYS186 4.9 29.0 1.0

Reference:

H.Li, C.S.Raman, P.Martasek, B.S.Masters, T.L.Poulos. Crystallographic Studies on Endothelial Nitric Oxide Synthase Complexed with Nitric Oxide and Mechanism-Based Inhibitors. Biochemistry V. 40 5399 2001.
ISSN: ISSN 0006-2960
PubMed: 11331003
DOI: 10.1021/BI002658V
Page generated: Sun Dec 13 14:14:09 2020

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