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Bromine in PDB 1rer: Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus.

Protein crystallography data

The structure of Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus., PDB code: 1rer was solved by D.L.Gibbons, M.C.Vaney, A.Roussel, A.Vigouroux, B.Reilly, M.Kielian, F.A.Rey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.20
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 198.197, 198.197, 116.250, 90.00, 90.00, 120.00
R / Rfree (%) 26.5 / 28.5

Other elements in 1rer:

The structure of Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus. also contains other interesting chemical elements:

Holmium (Ho) 4 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus. (pdb code 1rer). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus., PDB code: 1rer:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in 1rer

Go back to Bromine Binding Sites List in 1rer
Bromine binding site 1 out of 3 in the Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br417

b:95.1
occ:1.00
CA A:PRO191 3.3 51.4 1.0
CB A:PRO191 3.5 15.4 1.0
CG A:PRO191 3.8 15.4 1.0
N A:PRO191 4.2 50.9 1.0
CE1 A:PHE189 4.3 39.0 1.0
CG A:GLU45 4.3 64.2 1.0
C A:PRO191 4.4 52.6 1.0
N A:TYR192 4.4 88.9 1.0
NZ A:LYS123 4.6 45.9 1.0
CD A:GLU45 4.7 64.5 1.0
CD A:PRO191 4.7 15.9 1.0
NZ A:LYS176 4.7 48.7 1.0
OE2 A:GLU45 4.8 65.1 1.0
CE A:LYS123 4.8 44.9 1.0
CE A:LYS176 4.8 48.2 1.0
C A:PRO190 4.9 23.6 1.0
CD1 A:PHE189 4.9 40.3 1.0
O A:PHE189 5.0 70.3 1.0
O A:PRO190 5.0 23.2 1.0

Bromine binding site 2 out of 3 in 1rer

Go back to Bromine Binding Sites List in 1rer
Bromine binding site 2 out of 3 in the Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br418

b:77.7
occ:1.00
NZ B:LYS123 3.9 85.9 1.0
CE B:LYS123 4.0 83.8 1.0
CA B:PRO191 4.2 50.9 1.0
CE B:LYS176 4.2 63.6 1.0
NZ B:LYS176 4.3 63.2 1.0
CE1 B:PHE189 4.3 35.4 1.0
CB B:PRO191 4.3 20.7 1.0
CG B:PRO191 4.3 20.1 1.0
CD B:LYS176 4.5 63.1 1.0
CB C:ASP188 4.6 19.6 1.0
CG B:GLU45 4.6 65.0 1.0
CZ B:PHE189 4.8 35.6 1.0
CD B:GLU45 4.8 65.8 1.0
CD B:LYS123 4.8 82.6 1.0
N C:ASP188 4.8 32.6 1.0
N B:PRO191 4.9 49.1 1.0
OE2 B:GLU45 5.0 65.9 1.0

Bromine binding site 3 out of 3 in 1rer

Go back to Bromine Binding Sites List in 1rer
Bromine binding site 3 out of 3 in the Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Br416

b:84.0
occ:1.00
CA C:PRO191 3.9 16.6 1.0
CB C:PRO191 4.1 22.5 1.0
CE1 C:PHE189 4.1 31.4 1.0
CG C:PRO191 4.1 22.8 1.0
NZ C:LYS123 4.2 59.0 1.0
NZ C:LYS176 4.2 36.7 1.0
CE C:LYS176 4.3 36.5 1.0
CE C:LYS123 4.3 55.9 1.0
CG C:GLU45 4.5 84.3 1.0
N C:PRO191 4.6 16.9 1.0
CB A:ASP188 4.7 39.7 1.0
CD C:LYS176 4.7 36.1 1.0
CZ C:PHE189 4.7 31.7 1.0
CD C:GLU45 4.8 85.9 1.0
CD1 C:PHE189 4.8 31.6 1.0
O C:PHE189 4.9 62.5 1.0
C C:PRO191 4.9 19.2 1.0
OE2 C:GLU45 5.0 87.3 1.0
CD C:PRO191 5.0 23.0 1.0

Reference:

D.L.Gibbons, M.C.Vaney, A.Roussel, A.Vigouroux, B.Reilly, J.Lepault, M.Kielian, F.A.Rey. Conformational Change and Protein-Protein Interactions of the Fusion Protein of Semliki Forest Virus. Nature V. 427 320 2004.
ISSN: ISSN 0028-0836
PubMed: 14737160
DOI: 10.1038/NATURE02239
Page generated: Sat Dec 12 02:03:51 2020

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