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Iron in PDB 1fol: Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free)

Enzymatic activity of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free)

All present enzymatic activity of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free):
1.14.13.39;

Protein crystallography data

The structure of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free), PDB code: 1fol was solved by C.S.Raman, H.Li, P.Martasek, B.S.Masters, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.70 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.233, 106.282, 156.291, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 26.5

Other elements in 1fol:

The structure of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(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 Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free) (pdb code 1fol). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free), PDB code: 1fol:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1fol

Go back to Iron Binding Sites List in 1fol
Iron binding site 1 out of 2 in the Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:34.2
occ:1.00
FE A:HEM500 0.0 34.2 1.0
NA A:HEM500 2.0 34.5 1.0
ND A:HEM500 2.0 34.9 1.0
NC A:HEM500 2.0 34.0 1.0
NB A:HEM500 2.0 33.4 1.0
SG A:CYS186 2.3 35.5 1.0
C1A A:HEM500 3.0 35.2 1.0
C4C A:HEM500 3.0 34.6 1.0
C4A A:HEM500 3.0 34.8 1.0
C1B A:HEM500 3.0 32.8 1.0
C4D A:HEM500 3.0 35.3 1.0
C1D A:HEM500 3.0 34.7 1.0
C1C A:HEM500 3.1 34.2 1.0
C4B A:HEM500 3.1 33.6 1.0
CB A:CYS186 3.4 35.2 1.0
CHD A:HEM500 3.4 34.8 1.0
CHB A:HEM500 3.4 33.9 1.0
CHA A:HEM500 3.4 34.9 1.0
CHC A:HEM500 3.5 33.8 1.0
NH1 A:ARG1700 3.9 39.6 1.0
CA A:CYS186 4.0 35.1 1.0
C3D A:HEM500 4.3 35.5 1.0
C2A A:HEM500 4.3 35.4 1.0
C3A A:HEM500 4.3 35.0 1.0
C3C A:HEM500 4.3 34.3 1.0
C2D A:HEM500 4.3 35.2 1.0
C2B A:HEM500 4.3 32.9 1.0
C2C A:HEM500 4.3 34.1 1.0
C3B A:HEM500 4.3 33.4 1.0
CZ A:ARG1700 4.4 39.7 1.0
NE1 A:TRP180 4.4 32.7 1.0
CD A:ARG1700 4.8 39.9 1.0
NE A:ARG1700 4.8 39.6 1.0
C A:CYS186 4.9 35.2 1.0

Iron binding site 2 out of 2 in 1fol

Go back to Iron Binding Sites List in 1fol
Iron binding site 2 out of 2 in the Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Reduced Bovine Endothelial Nitric Oxide Synthase Heme Domain Complexed with L-Arg(H4B-Free) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:34.8
occ:1.00
FE B:HEM500 0.0 34.8 1.0
NB B:HEM500 1.9 33.6 1.0
ND B:HEM500 2.0 34.1 1.0
NA B:HEM500 2.0 34.6 1.0
NC B:HEM500 2.0 33.1 1.0
SG B:CYS186 2.2 34.5 1.0
C1B B:HEM500 3.0 33.8 1.0
C4B B:HEM500 3.0 33.8 1.0
C1D B:HEM500 3.0 34.0 1.0
C4D B:HEM500 3.0 35.0 1.0
C4C B:HEM500 3.0 33.1 1.0
C4A B:HEM500 3.0 34.8 1.0
C1C B:HEM500 3.0 33.5 1.0
C1A B:HEM500 3.1 35.1 1.0
CHB B:HEM500 3.4 34.2 1.0
CHC B:HEM500 3.4 33.5 1.0
CHD B:HEM500 3.4 33.5 1.0
NH1 B:ARG2700 3.5 37.5 1.0
CB B:CYS186 3.5 34.9 1.0
CHA B:HEM500 3.5 34.9 1.0
CZ B:ARG2700 4.1 37.5 1.0
CA B:CYS186 4.1 34.8 1.0
C2B B:HEM500 4.2 33.1 1.0
C2D B:HEM500 4.3 34.6 1.0
C3D B:HEM500 4.3 35.1 1.0
C3B B:HEM500 4.3 33.1 1.0
C3C B:HEM500 4.3 33.3 1.0
C2C B:HEM500 4.3 33.5 1.0
C2A B:HEM500 4.3 35.1 1.0
C3A B:HEM500 4.3 34.9 1.0
NE1 B:TRP180 4.4 33.0 1.0
NH2 B:ARG2700 4.5 37.5 1.0
NE B:ARG2700 4.7 37.0 1.0
C B:CYS186 4.9 34.8 1.0
N B:GLY188 4.9 34.6 1.0
N B:VAL187 4.9 34.5 1.0
CD B:ARG2700 4.9 36.1 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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