Manganese in PDB 3frx: Crystal Structure of the Yeast Orthologue of RACK1, ASC1.

The structure of Crystal Structure of the Yeast Orthologue of RACK1, ASC1., PDB code: 3frx was solved by S.M.Coyle, W.V.Gilbert, J.A.Doudna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.52 / 2.13
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	168.660, 85.410, 119.100, 90.00, 134.80, 90.00
R / Rfree (%)	19.5 / 23.9

The binding sites of Manganese atom in the Crystal Structure of the Yeast Orthologue of RACK1, ASC1. (pdb code 3frx). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of the Yeast Orthologue of RACK1, ASC1., PDB code: 3frx:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of the Yeast Orthologue of RACK1, ASC1.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Yeast Orthologue of RACK1, ASC1. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1138 b:34.6 occ:1.00 OD1 A:ASP114 2.4 9.8 1.0 O A:HOH515 2.4 22.6 1.0 O A:HOH527 2.4 27.1 1.0 O A:HOH353 2.5 44.6 1.0 O A:HOH345 2.5 20.6 1.0 O A:HOH794 2.6 27.0 1.0 CG A:ASP114 3.2 10.2 1.0 OD2 A:ASP114 3.4 15.8 1.0 O A:HOH1352 3.6 27.4 1.0 O A:ILE115 4.0 19.1 1.0 O A:HOH370 4.0 24.7 1.0 OG1 A:THR72 4.1 17.2 1.0 O A:HOH710 4.1 46.6 1.0 O A:HOH361 4.3 29.1 1.0 O A:HOH322 4.3 27.5 1.0 N A:ILE115 4.6 17.4 1.0 CB A:ASP114 4.7 12.1 1.0 O A:HOH1404 4.8 27.1 1.0 CG2 A:ILE115 4.9 22.6 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of the Yeast Orthologue of RACK1, ASC1.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the Yeast Orthologue of RACK1, ASC1. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1139 b:45.8 occ:1.00 OD1 B:ASP114 2.3 12.4 1.0 O B:HOH1422 2.5 26.8 1.0 O B:HOH749 2.5 32.7 1.0 O B:HOH407 2.5 23.9 1.0 O B:HOH610 2.7 33.1 1.0 O B:HOH420 3.0 29.9 1.0 CG B:ASP114 3.2 15.0 1.0 OD2 B:ASP114 3.4 17.1 1.0 OG1 B:THR72 3.7 19.6 1.0 O B:ILE115 4.1 13.7 1.0 O B:HOH411 4.2 27.2 1.0 O B:HOH1370 4.5 27.4 1.0 N B:ILE115 4.6 14.8 1.0 CB B:ASP114 4.6 17.5 1.0 CB B:THR72 4.7 12.7 1.0 CG2 B:ILE115 5.0 19.7 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of the Yeast Orthologue of RACK1, ASC1.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of the Yeast Orthologue of RACK1, ASC1. within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn1140 b:25.8 occ:1.00 O C:HOH327 2.3 16.2 1.0 OD1 C:ASP114 2.4 11.6 1.0 O C:HOH375 2.5 22.5 1.0 O C:HOH377 2.5 20.6 1.0 O C:HOH412 2.5 27.9 1.0 O C:HOH341 2.5 16.4 1.0 CG C:ASP114 3.3 14.7 1.0 OD2 C:ASP114 3.5 12.6 1.0 OG1 C:THR72 3.9 19.0 1.0 O C:ILE115 4.0 19.4 1.0 O C:HOH388 4.1 29.4 1.0 O C:HOH417 4.3 14.4 1.0 O C:HOH353 4.3 20.2 1.0 N C:ILE115 4.5 15.8 1.0 O C:HOH403 4.6 38.5 1.0 CB C:ASP114 4.7 12.6 1.0 CG2 C:ILE115 4.8 17.2 1.0 CB C:THR72 4.9 16.7 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of the Yeast Orthologue of RACK1, ASC1.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of the Yeast Orthologue of RACK1, ASC1. within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn1141 b:57.4 occ:1.00 OD1 D:ASP114 2.4 17.7 1.0 O D:HOH379 2.5 30.0 1.0 O D:HOH636 2.6 42.1 1.0 O D:HOH337 2.7 24.9 1.0 CG D:ASP114 3.3 13.7 1.0 OD2 D:ASP114 3.4 17.0 1.0 OG1 D:THR72 3.8 21.2 1.0 O D:ILE115 4.1 20.8 1.0 O D:HOH1306 4.1 27.4 1.0 O D:HOH1024 4.4 37.8 1.0 O D:HOH1399 4.6 27.1 1.0 N D:ILE115 4.7 14.4 1.0 O D:HOH366 4.7 29.0 1.0 CB D:ASP114 4.7 15.3 1.0 CB D:THR72 4.8 17.1 1.0 O D:HOH785 4.9 40.6 1.0

S.M.Coyle, W.V.Gilbert, J.A.Doudna. Direct Link Between RACK1 Function and Localization at the Ribosome in Vivo Mol.Cell.Biol. V. 29 1626 2009.
ISSN: ISSN 0270-7306
PubMed: 19114558
DOI: 10.1128/MCB.01718-08