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Iron in PDB 1nse: Bovine Endothelial Nitric Oxide Synthase

Enzymatic activity of Bovine Endothelial Nitric Oxide Synthase

All present enzymatic activity of Bovine Endothelial Nitric Oxide Synthase:
1.14.13.39;

Protein crystallography data

The structure of Bovine Endothelial Nitric Oxide Synthase, PDB code: 1nse was solved by C.S.Raman, H.Li, P.Martasek, V.Kral, 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) 10.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.000, 106.550, 156.220, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 27.8

Other elements in 1nse:

The structure of Bovine Endothelial Nitric Oxide Synthase 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 (pdb code 1nse). 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, PDB code: 1nse:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1nse

Go back to Iron Binding Sites List in 1nse
Iron binding site 1 out of 2 in the Bovine Endothelial Nitric Oxide Synthase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:18.5
occ:1.00
FE A:HEM500 0.0 18.5 1.0
NB A:HEM500 2.0 10.9 1.0
ND A:HEM500 2.0 12.6 1.0
NA A:HEM500 2.0 23.9 1.0
NC A:HEM500 2.0 18.3 1.0
SG A:CYS186 2.3 17.0 1.0
C4B A:HEM500 3.0 17.4 1.0
C1A A:HEM500 3.0 9.1 1.0
C1D A:HEM500 3.0 19.8 1.0
C1C A:HEM500 3.0 10.5 1.0
C4D A:HEM500 3.0 19.4 1.0
C1B A:HEM500 3.0 19.1 1.0
C4C A:HEM500 3.1 12.8 1.0
C4A A:HEM500 3.1 13.4 1.0
CB A:CYS186 3.3 14.5 1.0
CHC A:HEM500 3.4 13.8 1.0
CHA A:HEM500 3.4 12.1 1.0
CHD A:HEM500 3.5 17.2 1.0
CHB A:HEM500 3.5 16.8 1.0
C2 A:ITU800 3.8 13.0 1.0
CA A:CYS186 4.1 13.1 1.0
S A:ITU800 4.1 22.7 1.0
C2B A:HEM500 4.2 11.9 1.0
C3B A:HEM500 4.3 19.1 1.0
C2D A:HEM500 4.3 18.3 1.0
C2C A:HEM500 4.3 14.6 1.0
C3D A:HEM500 4.3 15.9 1.0
C2A A:HEM500 4.3 18.8 1.0
C3C A:HEM500 4.3 14.8 1.0
C3A A:HEM500 4.3 15.7 1.0
NE1 A:TRP180 4.3 11.9 1.0
C3 A:ITU800 4.6 20.3 1.0
N A:GLY188 4.7 17.0 1.0
N1 A:ITU800 4.8 20.7 1.0
C A:CYS186 4.8 14.5 1.0
CD1 A:TRP180 4.8 9.4 1.0
O A:HOH1101 4.9 23.0 1.0
N A:VAL187 4.9 11.2 1.0

Iron binding site 2 out of 2 in 1nse

Go back to Iron Binding Sites List in 1nse
Iron binding site 2 out of 2 in the Bovine Endothelial Nitric Oxide Synthase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:19.6
occ:1.00
FE B:HEM500 0.0 19.6 1.0
NB B:HEM500 2.0 16.8 1.0
ND B:HEM500 2.0 16.8 1.0
NA B:HEM500 2.0 22.3 1.0
NC B:HEM500 2.0 15.1 1.0
SG B:CYS186 2.3 20.5 1.0
C1D B:HEM500 3.0 24.8 1.0
C4C B:HEM500 3.0 11.8 1.0
C4D B:HEM500 3.0 19.0 1.0
C1A B:HEM500 3.0 18.5 1.0
C4B B:HEM500 3.0 21.3 1.0
C1B B:HEM500 3.0 15.7 1.0
C4A B:HEM500 3.0 15.1 1.0
C1C B:HEM500 3.1 16.1 1.0
CB B:CYS186 3.4 18.5 1.0
CHD B:HEM500 3.4 16.9 1.0
CHC B:HEM500 3.4 17.2 1.0
CHA B:HEM500 3.4 17.8 1.0
CHB B:HEM500 3.5 14.4 1.0
C2 B:ITU800 3.7 15.8 1.0
S B:ITU800 4.0 21.0 1.0
CA B:CYS186 4.1 19.2 1.0
C2D B:HEM500 4.3 26.7 1.0
C3D B:HEM500 4.3 24.6 1.0
C3C B:HEM500 4.3 20.0 1.0
NE1 B:TRP180 4.3 21.0 1.0
C2C B:HEM500 4.3 18.4 1.0
C3B B:HEM500 4.3 22.7 1.0
C2B B:HEM500 4.3 20.8 1.0
C2A B:HEM500 4.3 24.6 1.0
C3A B:HEM500 4.3 23.8 1.0
C3 B:ITU800 4.6 28.2 1.0
N1 B:ITU800 4.7 22.8 1.0
N B:GLY188 4.8 21.3 1.0
C B:CYS186 4.8 8.5 1.0
CD1 B:TRP180 4.9 18.0 1.0
N B:VAL187 4.9 17.2 1.0
O B:HOH976 5.0 21.6 1.0

Reference:

C.S.Raman, H.Li, P.Martasek, V.Kral, B.S.Masters, T.L.Poulos. Crystal Structure of Constitutive Endothelial Nitric Oxide Synthase: A Paradigm For Pterin Function Involving A Novel Metal Center. Cell(Cambridge,Mass.) V. 95 939 1998.
ISSN: ISSN 0092-8674
PubMed: 9875848
DOI: 10.1016/S0092-8674(00)81718-3
Page generated: Sun Dec 13 14:26:02 2020

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