Magnesium in PDB 3doe: Complex of ARL2 and Bart, Crystal Form 1

The structure of Complex of ARL2 and Bart, Crystal Form 1, PDB code: 3doe was solved by T.Zhang, S.Li, J.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.90 / 2.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.827, 44.081, 66.495, 90.00, 111.46, 90.00
R / Rfree (%)	23 / 26.1

The binding sites of Magnesium atom in the Complex of ARL2 and Bart, Crystal Form 1 (pdb code 3doe). 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 Complex of ARL2 and Bart, Crystal Form 1, PDB code: 3doe:

Magnesium binding site 1 out of 1 in the Complex of ARL2 and Bart, Crystal Form 1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Complex of ARL2 and Bart, Crystal Form 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg193 b:28.9 occ:1.00 O A:HOH220 2.1 24.3 1.0 O A:HOH209 2.2 22.9 1.0 OG1 A:THR30 2.2 22.9 1.0 O2G A:GTP201 2.2 28.6 1.0 OG1 A:THR47 2.3 28.2 1.0 O2B A:GTP201 2.3 24.7 1.0 CB A:THR30 3.0 22.3 1.0 PG A:GTP201 3.3 28.5 1.0 CB A:THR47 3.4 28.2 1.0 PB A:GTP201 3.4 26.4 1.0 O3B A:GTP201 3.5 26.6 1.0 N A:THR47 3.6 30.7 1.0 O3G A:GTP201 3.8 29.0 1.0 O2A A:GTP201 3.9 24.9 1.0 N A:THR30 4.0 21.8 1.0 CG2 A:THR30 4.0 22.7 1.0 OD2 A:ASP66 4.0 22.2 1.0 CA A:THR30 4.1 22.1 1.0 CA A:THR47 4.1 28.6 1.0 O A:SER45 4.2 37.1 1.0 O A:HOH273 4.2 25.9 1.0 OD1 A:ASP66 4.3 21.4 1.0 O3A A:GTP201 4.5 24.4 1.0 O1B A:GTP201 4.5 24.2 1.0 PA A:GTP201 4.5 25.3 1.0 O1A A:GTP201 4.5 24.8 1.0 C A:PRO46 4.5 32.1 1.0 O1G A:GTP201 4.6 28.8 1.0 CG2 A:THR47 4.6 27.9 1.0 CG A:ASP66 4.6 21.7 1.0 CA A:PRO46 4.6 33.1 1.0 ND2 A:ASN51 4.7 28.8 1.0

T.Zhang, S.Li, Y.Zhang, C.Zhong, Z.Lai, J.Ding. Crystal Structure of the ARL2-Gtp-Bart Complex Reveals A Novel Recognition and Binding Mode of Small Gtpase with Effector Structure V. 17 602 2009.
ISSN: ISSN 0969-2126
PubMed: 19368893
DOI: 10.1016/J.STR.2009.01.014