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Magnesium in PDB 4wfm: Structure of the Complete Bacterial Srp Alu Domain

Protein crystallography data

The structure of Structure of the Complete Bacterial Srp Alu Domain, PDB code: 4wfm was solved by G.Kempf, K.Wild, I.Sinning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.55 / 3.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 176.254, 194.345, 82.992, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 20.8

Other elements in 4wfm:

The structure of Structure of the Complete Bacterial Srp Alu Domain also contains other interesting chemical elements:

Cobalt (Co) 23 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Complete Bacterial Srp Alu Domain (pdb code 4wfm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of the Complete Bacterial Srp Alu Domain, PDB code: 4wfm:

Magnesium binding site 1 out of 1 in 4wfm

Go back to Magnesium Binding Sites List in 4wfm
Magnesium binding site 1 out of 1 in the Structure of the Complete Bacterial Srp Alu Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Complete Bacterial Srp Alu Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg212

b:0.6
occ:1.00
O B:HOH302 2.1 0.8 1.0
O2A B:GTP3 2.2 0.6 1.0
O3G B:GTP3 2.3 0.5 1.0
O B:HOH301 2.4 72.4 1.0
N5 B:NCO209 2.8 0.1 1.0
N4 B:NCO209 3.4 0.3 1.0
PA B:GTP3 3.5 99.9 1.0
PG B:GTP3 3.7 0.6 1.0
O1A B:GTP3 3.7 99.8 1.0
CO B:NCO209 4.1 0.9 1.0
N1 B:NCO209 4.2 0.7 1.0
O3B B:GTP3 4.2 0.2 1.0
O3A B:GTP3 4.3 0.7 1.0
O2G B:GTP3 4.4 0.6 1.0
O B:HOH303 4.5 69.4 1.0
O5' B:GTP3 4.7 70.3 1.0
O1G B:GTP3 4.7 0.4 1.0
C5' B:GTP3 4.7 71.6 1.0
N2 B:NCO209 4.9 55.2 1.0
PB B:GTP3 5.0 0.9 1.0

Reference:

G.Kempf, K.Wild, I.Sinning. Structure of the Complete Bacterial Srp Alu Domain. Nucleic Acids Res. V. 42 12284 2014.
ISSN: ESSN 1362-4962
PubMed: 25270875
DOI: 10.1093/NAR/GKU883
Page generated: Tue Aug 20 13:33:49 2024

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