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Praseodymium in PDB 4bd8: Bax Domain Swapped Dimer Induced By BIMBH3 with Chaps

Protein crystallography data

The structure of Bax Domain Swapped Dimer Induced By BIMBH3 with Chaps, PDB code: 4bd8 was solved by P.E.Czabotar, D.Westphal, J.M.Adams, P.M.Colman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.823 / 2.22
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 142.947, 142.947, 86.712, 90.00, 90.00, 120.00
R / Rfree (%) 19.72 / 25.55

Praseodymium Binding Sites:

The binding sites of Praseodymium atom in the Bax Domain Swapped Dimer Induced By BIMBH3 with Chaps (pdb code 4bd8). This binding sites where shown within 5.0 Angstroms radius around Praseodymium atom.
In total 2 binding sites of Praseodymium where determined in the Bax Domain Swapped Dimer Induced By BIMBH3 with Chaps, PDB code: 4bd8:
Jump to Praseodymium binding site number: 1; 2;

Praseodymium binding site 1 out of 2 in 4bd8

Go back to Praseodymium Binding Sites List in 4bd8
Praseodymium binding site 1 out of 2 in the Bax Domain Swapped Dimer Induced By BIMBH3 with Chaps


Mono view


Stereo pair view

A full contact list of Praseodymium with other atoms in the Pr binding site number 1 of Bax Domain Swapped Dimer Induced By BIMBH3 with Chaps within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pr1171

b:56.6
occ:1.00
O A:HOH2069 2.7 47.1 1.0
OD1 A:ASP142 2.7 56.8 1.0
OD2 A:ASP142 2.9 54.2 1.0
OE2 A:GLU146 3.0 87.2 1.0
CG A:ASP142 3.2 50.4 1.0
CD A:GLU146 3.9 85.2 1.0
CG A:GLU146 4.4 63.8 1.0
CB A:ASP142 4.7 44.0 1.0
OE1 A:GLU146 4.7 77.0 1.0

Praseodymium binding site 2 out of 2 in 4bd8

Go back to Praseodymium Binding Sites List in 4bd8
Praseodymium binding site 2 out of 2 in the Bax Domain Swapped Dimer Induced By BIMBH3 with Chaps


Mono view


Stereo pair view

A full contact list of Praseodymium with other atoms in the Pr binding site number 2 of Bax Domain Swapped Dimer Induced By BIMBH3 with Chaps within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pr1171

b:76.0
occ:1.00
OD1 B:ASP142 2.8 67.3 1.0
OD2 B:ASP142 2.8 69.0 1.0
OE2 B:GLU146 2.8 94.1 1.0
OE1 B:GLU146 2.9 83.6 1.0
CG B:ASP142 3.1 64.4 1.0
CD B:GLU146 3.2 84.7 1.0
O B:HOH2045 3.3 92.5 1.0
O B:HOH2046 4.1 75.9 1.0
O B:HOH2048 4.5 77.7 1.0
CG B:GLU146 4.6 76.8 1.0
CB B:ASP142 4.6 60.3 1.0
OE2 C:GLU69 4.9 0.8 1.0

Reference:

P.E.Czabotar, D.Westphal, G.Dewson, S.Ma, C.Hockings, W.D.Fairlie, E.F.Lee, S.Yao, A.Y.Robin, B.J.Smith, D.C.Huang, R.M.Kluck, J.M.Adams, P.M.Colman. Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis. Cell(Cambridge,Mass.) V. 152 519 2013.
ISSN: ISSN 0092-8674
PubMed: 23374347
DOI: 10.1016/J.CELL.2012.12.031
Page generated: Thu Oct 29 06:39:26 2020

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