Magnesium in PDB 1re0: Structure of ARF1-Gdp Bound to SEC7 Domain Complexed with Brefeldin A

The structure of Structure of ARF1-Gdp Bound to SEC7 Domain Complexed with Brefeldin A, PDB code: 1re0 was solved by J.Goldberg, E.Mossessova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.95 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.725, 72.294, 119.632, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 23.4

The binding sites of Magnesium atom in the Structure of ARF1-Gdp Bound to SEC7 Domain Complexed with Brefeldin A (pdb code 1re0). 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 ARF1-Gdp Bound to SEC7 Domain Complexed with Brefeldin A, PDB code: 1re0:

Magnesium binding site 1 out of 1 in the Structure of ARF1-Gdp Bound to SEC7 Domain Complexed with Brefeldin A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of ARF1-Gdp Bound to SEC7 Domain Complexed with Brefeldin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg701 b:42.6 occ:1.00 OG1 A:THR31 1.8 34.5 1.0 O A:HOH742 2.1 26.4 1.0 O A:HOH743 2.1 32.6 1.0 O2B A:GDP700 2.1 32.3 1.0 O A:HOH705 2.1 32.1 1.0 O A:HOH704 2.2 32.5 1.0 CB A:THR31 3.1 36.9 1.0 PB A:GDP700 3.3 33.1 1.0 O3B A:GDP700 3.5 30.2 1.0 O A:HOH736 3.8 31.9 1.0 N A:THR31 3.8 33.4 1.0 CA A:THR31 4.0 34.8 1.0 OE2 A:GLU54 4.0 41.2 1.0 CG2 A:THR31 4.2 33.0 1.0 OE1 A:GLU54 4.2 45.0 1.0 O2A A:GDP700 4.3 37.4 1.0 O1B A:GDP700 4.3 31.2 1.0 O3A A:GDP700 4.3 34.2 1.0 CD A:GLU54 4.5 42.2 1.0 PA A:GDP700 4.7 38.1 1.0 O A:HOH732 4.8 49.7 1.0 O1A A:GDP700 4.9 34.8 1.0 CB A:LYS30 4.9 27.7 1.0 C A:LYS30 4.9 31.6 1.0

E.Mossessova, R.A.Corpina, J.Goldberg. Crystal Structure of ARF1*SEC7 Complexed with Brefeldin A and Its Implications For the Guanine Nucleotide Exchange Mechanism. Mol.Cell V. 12 1403 2003.
ISSN: ISSN 1097-2765
PubMed: 14690595
DOI: 10.1016/S1097-2765(03)00475-1