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

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

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

Bromine

(Br)

3 atoms

The binding sites of Holmium 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 Holmium atom.
In total 4 binding sites of Holmium where determined in the Crystal Structure of the Homotrimer of Fusion Glycoprotein E1 From Semliki Forest Virus., PDB code: 1rer:
Jump to Holmium binding site number: 1; 2; 3; 4;

Holmium binding site 1 out of 4 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 Holmium with other atoms in the Ho 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:Ho411 b:18.6 occ:1.00 OD2 C:ASP188 1.8 16.4 1.0 OD2 A:ASP188 1.8 36.5 1.0 OD2 B:ASP188 1.9 63.5 1.0 OD1 C:ASP188 2.1 18.4 1.0 OD1 A:ASP188 2.2 39.9 1.0 OD1 B:ASP188 2.2 65.0 1.0 CG C:ASP188 2.3 19.2 1.0 CG A:ASP188 2.3 39.9 1.0 CG B:ASP188 2.3 64.6 1.0 O C:HOH455 3.0 32.4 1.0 O A:HOH460 3.7 26.3 1.0 CB C:ASP188 3.8 19.6 1.0 NZ C:LYS176 3.8 36.7 1.0 NZ A:LYS176 3.9 48.7 1.0 CB A:ASP188 3.9 39.7 1.0 NZ B:LYS176 3.9 63.2 1.0 CB B:ASP188 3.9 64.0 1.0 O C:ASP188 4.7 32.5 1.0 O B:ASP188 4.8 84.4 1.0 O A:ASP188 4.8 64.2 1.0 CA C:ASP188 4.8 32.7 1.0 CA A:ASP188 4.9 64.3 1.0 CA B:ASP188 4.9 83.8 1.0 CE C:LYS176 5.0 36.5 1.0

Holmium binding site 2 out of 4 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 Holmium with other atoms in the Ho 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 A:Ho412 b:67.5 occ:1.00 N A:ALA391 2.3 0.3 1.0 CA A:ALA391 2.5 0.8 1.0 OXT A:ALA391 2.5 97.7 1.0 C A:ALA391 2.6 0.9 1.0 CB A:ALA391 2.7 97.8 1.0 C A:TYR390 3.3 0.9 1.0 OE2 C:GLU72 3.3 95.4 1.0 O A:ALA391 3.5 0.2 1.0 OE1 C:GLU72 3.7 97.7 1.0 O A:HOH468 3.7 42.9 1.0 O C:HOH440 3.8 40.7 1.0 CD C:GLU72 3.9 97.1 1.0 CA A:TYR390 3.9 0.5 1.0 O A:TYR390 4.2 0.0 1.0 O A:PRO389 4.3 72.8 1.0 CG A:TYR390 4.7 0.7 1.0 CD2 A:TYR390 4.8 0.3 1.0 CB A:TYR390 4.8 0.3 1.0

Holmium binding site 3 out of 4 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 Holmium with other atoms in the Ho 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 B:Ho413 b:77.7 occ:1.00 N B:ALA391 2.4 0.1 1.0 OE1 A:GLU72 2.7 0.6 1.0 CA B:ALA391 2.8 0.5 1.0 CB B:ALA391 2.9 86.4 1.0 OXT B:ALA391 3.0 86.3 1.0 C B:ALA391 3.1 0.2 1.0 C B:TYR390 3.4 0.8 1.0 OE2 A:GLU72 3.4 0.1 1.0 CD A:GLU72 3.4 0.1 1.0 O A:HOH469 3.5 42.8 1.0 CA B:TYR390 3.8 0.3 1.0 O B:PRO389 4.1 73.0 1.0 O B:ALA391 4.1 0.8 1.0 O B:TYR390 4.4 0.0 1.0 CG B:TYR390 4.6 0.4 1.0 CB B:TYR390 4.7 0.7 1.0 CD2 B:TYR390 4.8 0.7 1.0 N B:TYR390 4.8 0.3 1.0 C B:PRO389 4.9 72.2 1.0 CG A:GLU72 4.9 0.1 1.0

Holmium binding site 4 out of 4 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 Holmium with other atoms in the Ho binding site number 4 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:Ho414 b:69.9 occ:1.00 N C:ALA391 2.4 0.6 1.0 CA C:ALA391 2.7 0.5 1.0 CB C:ALA391 2.8 45.1 1.0 OXT C:ALA391 2.9 44.6 1.0 C C:ALA391 3.0 0.6 1.0 OE1 B:GLU72 3.4 0.9 1.0 C C:TYR390 3.4 90.7 1.0 CA C:TYR390 3.9 87.7 1.0 O C:ALA391 3.9 0.9 1.0 OE2 B:GLU72 4.1 0.4 1.0 CD B:GLU72 4.1 0.6 1.0 O C:PRO389 4.2 58.6 1.0 O C:TYR390 4.4 89.3 1.0 CG C:TYR390 4.8 88.3 1.0 CB C:TYR390 4.8 87.7 1.0 CD2 C:TYR390 4.9 87.6 1.0 N C:TYR390 5.0 84.9 1.0

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