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Magnesium in PDB 2w58: Crystal Structure of the Dnai

Protein crystallography data

The structure of Crystal Structure of the Dnai, PDB code: 2w58 was solved by K.L.Tsai, Y.H.Lo, Y.J.Sun, C.D.Hsiao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.77 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.632, 59.530, 115.636, 90.00, 90.00, 90.00
R / Rfree (%) 23.5 / 26.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Dnai (pdb code 2w58). 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 Crystal Structure of the Dnai, PDB code: 2w58:

Magnesium binding site 1 out of 1 in 2w58

Go back to Magnesium Binding Sites List in 2w58
Magnesium binding site 1 out of 1 in the Crystal Structure of the Dnai


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Dnai within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1311

b:41.8
occ:1.00
O A:HOH2073 2.3 19.8 1.0
O A:HOH2074 2.4 34.5 1.0
OG1 A:THR175 2.5 19.7 1.0
O A:HOH2045 2.5 26.9 1.0
PB A:ADP1310 3.1 33.7 1.0
O2B A:ADP1310 3.2 53.2 1.0
O3B A:ADP1310 3.3 36.5 1.0
CB A:THR175 3.8 29.7 1.0
OD2 A:ASP229 3.9 43.5 1.0
O A:HOH2046 4.0 51.1 1.0
O1A A:ADP1310 4.2 51.5 1.0
OD1 A:ASP229 4.2 32.9 1.0
N A:THR175 4.3 24.1 1.0
O1B A:ADP1310 4.4 45.0 1.0
O3A A:ADP1310 4.4 40.9 1.0
CG A:ASP229 4.5 41.0 1.0
CA A:THR175 4.6 33.3 1.0
O B:HOH2071 4.6 49.4 1.0
CE A:LYS174 4.7 19.9 1.0
PA A:ADP1310 4.7 41.7 1.0
NZ A:LYS174 4.7 10.7 1.0
OG1 A:THR262 4.8 32.9 1.0
CG2 A:THR175 4.8 26.8 1.0
O2A A:ADP1310 4.8 33.5 1.0
CB A:LYS174 4.9 23.0 1.0

Reference:

K.L.Tsai, Y.H.Lo, Y.J.Sun, C.D.Hsiao. Molecular Interplay Between the Replicative Helicase Dnac and Its Loader Protein Dnai From Geobacillus Kaustophilus. J.Mol.Biol. V. 393 1056 2009.
ISSN: ISSN 0022-2836
PubMed: 19744498
DOI: 10.1016/J.JMB.2009.09.002
Page generated: Mon Dec 14 07:43:30 2020

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