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Praseodymium in PDB 4wt0: Crystal Structure of the Dna Binding Domains of LIARD191N From E. Faecalis

Protein crystallography data

The structure of Crystal Structure of the Dna Binding Domains of LIARD191N From E. Faecalis, PDB code: 4wt0 was solved by M.Davlieva, Y.Shamoo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.79 / 1.80
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 31.049, 76.934, 76.920, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 24.6

Praseodymium Binding Sites:

The binding sites of Praseodymium atom in the Crystal Structure of the Dna Binding Domains of LIARD191N From E. Faecalis (pdb code 4wt0). This binding sites where shown within 5.0 Angstroms radius around Praseodymium atom.
In total 2 binding sites of Praseodymium where determined in the Crystal Structure of the Dna Binding Domains of LIARD191N From E. Faecalis, PDB code: 4wt0:
Jump to Praseodymium binding site number: 1; 2;

Praseodymium binding site 1 out of 2 in 4wt0

Go back to Praseodymium Binding Sites List in 4wt0
Praseodymium binding site 1 out of 2 in the Crystal Structure of the Dna Binding Domains of LIARD191N From E. Faecalis


Mono view


Stereo pair view

A full contact list of Praseodymium with other atoms in the Pr binding site number 1 of Crystal Structure of the Dna Binding Domains of LIARD191N From E. Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pr300

b:26.2
occ:1.00
OD2 B:ASP190 2.5 24.8 1.0
OD1 B:ASP190 2.7 16.1 1.0
CG B:ASP190 2.9 18.4 1.0
O B:HOH409 3.1 39.8 1.0
O B:HOH418 4.0 10.2 1.0
CB B:ASP190 4.4 20.1 1.0
O B:HOH415 4.7 19.0 1.0
O A:HOH407 4.8 17.9 1.0
OE1 B:GLN194 4.8 18.6 1.0
O B:HOH469 5.0 25.0 1.0
NE2 B:GLN194 5.0 21.3 1.0

Praseodymium binding site 2 out of 2 in 4wt0

Go back to Praseodymium Binding Sites List in 4wt0
Praseodymium binding site 2 out of 2 in the Crystal Structure of the Dna Binding Domains of LIARD191N From E. Faecalis


Mono view


Stereo pair view

A full contact list of Praseodymium with other atoms in the Pr binding site number 2 of Crystal Structure of the Dna Binding Domains of LIARD191N From E. Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pr300

b:24.0
occ:1.00
O A:HOH409 2.6 45.6 1.0
O A:HOH408 2.7 35.1 1.0
OD2 A:ASP190 2.8 9.4 1.0
CG A:ASP190 3.3 9.1 1.0
OD1 A:ASP190 3.3 17.7 1.0
OE1 A:GLN194 4.4 11.9 1.0
CB A:ASP190 4.5 8.5 1.0
N A:ASP190 4.8 14.9 1.0
NE2 A:GLN194 4.8 16.1 1.0
O A:HOH417 5.0 10.4 1.0

Reference:

M.Davlieva, Y.Shi, P.G.Leonard, T.A.Johnson, M.R.Zianni, C.A.Arias, J.E.Ladbury, Y.Shamoo. A Variable Dna Recognition Site Organization Establishes the Liar-Mediated Cell Envelope Stress Response of Enterococci to Daptomycin. Nucleic Acids Res. 2015.
ISSN: ESSN 1362-4962
PubMed: 25897118
DOI: 10.1093/NAR/GKV321
Page generated: Wed Dec 16 02:03:06 2020

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