Atomistry » Iron » PDB 2aiu-2axx » 2amo
Atomistry »
  Iron »
    PDB 2aiu-2axx »
      2amo »

Iron in PDB 2amo: Loose Dimer of A Bacillus Subtilis Nitric Oxide Synthase

Enzymatic activity of Loose Dimer of A Bacillus Subtilis Nitric Oxide Synthase

All present enzymatic activity of Loose Dimer of A Bacillus Subtilis Nitric Oxide Synthase:
1.14.13.39;

Protein crystallography data

The structure of Loose Dimer of A Bacillus Subtilis Nitric Oxide Synthase, PDB code: 2amo was solved by K.Pant, B.R.Crane, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.62 / 2.60
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 81.314, 93.211, 118.546, 90.00, 90.00, 90.00
R / Rfree (%) 27.4 / 29

Iron Binding Sites:

The binding sites of Iron atom in the Loose Dimer of A Bacillus Subtilis Nitric Oxide Synthase (pdb code 2amo). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Loose Dimer of A Bacillus Subtilis Nitric Oxide Synthase, PDB code: 2amo:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2amo

Go back to Iron Binding Sites List in 2amo
Iron binding site 1 out of 2 in the Loose Dimer of A Bacillus Subtilis 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 Loose Dimer of A Bacillus Subtilis Nitric Oxide Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1901

b:23.9
occ:0.97
FE A:HEM1901 0.0 23.9 1.0
NA A:HEM1901 2.0 22.8 1.0
NC A:HEM1901 2.0 22.5 1.0
ND A:HEM1901 2.1 18.7 1.0
NB A:HEM1901 2.1 17.8 1.0
SG A:CYS62 2.2 22.1 1.0
C1A A:HEM1901 3.0 24.4 1.0
C1C A:HEM1901 3.1 20.8 1.0
C4A A:HEM1901 3.1 24.7 1.0
C4B A:HEM1901 3.1 16.8 1.0
C4C A:HEM1901 3.1 20.0 1.0
C4D A:HEM1901 3.1 22.0 1.0
C1B A:HEM1901 3.1 18.6 1.0
C1D A:HEM1901 3.1 21.1 1.0
CB A:CYS62 3.4 26.0 1.0
CHC A:HEM1901 3.4 20.8 1.0
CHA A:HEM1901 3.4 22.0 1.0
CHB A:HEM1901 3.5 22.2 1.0
CHD A:HEM1901 3.5 14.9 1.0
CA A:CYS62 4.3 26.8 1.0
C3A A:HEM1901 4.3 23.0 1.0
C2A A:HEM1901 4.3 22.2 1.0
C3B A:HEM1901 4.3 18.9 1.0
C2C A:HEM1901 4.3 21.8 1.0
C2B A:HEM1901 4.3 21.2 1.0
C3C A:HEM1901 4.4 21.1 1.0
C3D A:HEM1901 4.4 20.6 1.0
C2D A:HEM1901 4.4 24.8 1.0
NE1 A:TRP56 4.4 28.2 1.0

Iron binding site 2 out of 2 in 2amo

Go back to Iron Binding Sites List in 2amo
Iron binding site 2 out of 2 in the Loose Dimer of A Bacillus Subtilis 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 Loose Dimer of A Bacillus Subtilis Nitric Oxide Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1902

b:56.3
occ:0.63
FE B:HEM1902 0.0 56.3 0.6
NA B:HEM1902 2.1 54.7 0.6
NB B:HEM1902 2.1 56.1 0.6
SG B:CYS62 2.1 68.6 0.8
NC B:HEM1902 2.1 53.9 0.6
ND B:HEM1902 2.1 56.4 0.6
CB B:CYS62 3.1 73.3 0.8
C1A B:HEM1902 3.1 57.3 0.6
C4B B:HEM1902 3.1 53.7 0.6
C4A B:HEM1902 3.1 52.9 0.6
C1B B:HEM1902 3.1 56.5 0.6
C4C B:HEM1902 3.1 52.3 0.6
C1C B:HEM1902 3.1 54.5 0.6
C4D B:HEM1902 3.1 54.4 0.6
C1D B:HEM1902 3.2 55.5 0.6
CHA B:HEM1902 3.5 54.5 0.6
CHC B:HEM1902 3.5 54.5 0.6
CHB B:HEM1902 3.5 56.1 0.6
CHD B:HEM1902 3.5 52.9 0.6
CA B:CYS62 3.8 73.7 0.8
C2A B:HEM1902 4.3 60.5 0.6
C3A B:HEM1902 4.3 56.1 0.6
C3B B:HEM1902 4.3 56.2 0.6
O B:HOH737 4.3 33.2 1.0
C2C B:HEM1902 4.3 51.8 0.6
C3C B:HEM1902 4.3 52.8 0.6
C2B B:HEM1902 4.4 53.8 0.6
C3D B:HEM1902 4.4 55.5 0.6
C2D B:HEM1902 4.4 56.0 0.6
NE1 B:TRP56 4.4 73.6 0.8
N B:ILE63 4.5 76.2 0.8
C B:CYS62 4.6 74.8 0.8
N B:GLY64 4.7 77.0 0.8
N B:CYS62 5.0 73.1 0.8

Reference:

K.Pant, B.R.Crane. Structure of A Loose Dimer: An Intermediate in Nitric Oxide Synthase Assembly. J.Mol.Biol. V. 352 932 2005.
ISSN: ISSN 0022-2836
PubMed: 16126221
DOI: 10.1016/J.JMB.2005.07.070
Page generated: Sat Aug 3 19:19:40 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy