Magnesium in PDB 2r75: Aquifex Aeolicus Ftsz with 8-Morpholino-Gtp

The structure of Aquifex Aeolicus Ftsz with 8-Morpholino-Gtp, PDB code: 2r75 was solved by T.Lappchen, V.A.Pinas, A.F.Hartog, G.J.Koomen, C.Schaffner-Barbero, J.M.Andreu, D.Trambaiolo, J.Lowe, A.Juhem, A.V.Popov, T.Den Blaauwen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.85 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.846, 74.177, 44.197, 90.00, 95.08, 90.00
R / Rfree (%)	13.7 / 18.4

The binding sites of Magnesium atom in the Aquifex Aeolicus Ftsz with 8-Morpholino-Gtp (pdb code 2r75). 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 Aquifex Aeolicus Ftsz with 8-Morpholino-Gtp, PDB code: 2r75:

Magnesium binding site 1 out of 1 in the Aquifex Aeolicus Ftsz with 8-Morpholino-Gtp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Aquifex Aeolicus Ftsz with 8-Morpholino-Gtp within 5.0Å range: probe atom residue distance (Å) B Occ 1:Mg615 b:13.9 occ:1.00 O 1:HOH750 2.0 17.8 1.0 O 1:HOH817 2.1 18.2 1.0 O2G 1:01G614 2.1 14.2 1.0 O 1:HOH623 2.1 12.4 1.0 O 1:HOH649 2.3 15.0 1.0 O2B 1:01G614 2.3 7.7 1.0 PG 1:01G614 3.3 12.1 1.0 PB 1:01G614 3.4 7.7 1.0 O3G 1:01G614 3.6 11.1 1.0 O3B 1:01G614 3.6 8.5 1.0 O 1:HOH807 3.8 52.5 1.0 O3A 1:01G614 3.9 8.1 1.0 OD2 1:ASP42 4.0 17.2 1.0 O2A 1:01G614 4.0 14.1 1.0 OD1 1:ASN40 4.3 10.2 1.0 N 1:GLY17 4.3 7.4 1.0 CB 1:ASP42 4.4 11.6 1.0 ND2 1:ASN40 4.6 11.0 1.0 PA 1:01G614 4.6 9.2 1.0 O1G 1:01G614 4.6 12.4 1.0 CA 1:GLY17 4.6 8.5 1.0 O1B 1:01G614 4.7 9.1 1.0 CG 1:ASP42 4.7 12.2 1.0 CG 1:ASN40 4.9 10.7 1.0 O 1:HOH724 4.9 29.9 1.0

T.Lappchen, V.A.Pinas, A.F.Hartog, G.J.Koomen, C.Schaffner-Barbero, J.M.Andreu, D.Trambaiolo, J.Lowe, A.Juhem, A.V.Popov, T.Den Blaauwen. Probing Ftsz and Tubulin with C8-Substituted Gtp Analogs Reveals Differences in Their Nucleotide Binding Sites Chem.Biol. V. 15 189 2008.
ISSN: ISSN 1074-5521
PubMed: 18291323
DOI: 10.1016/J.CHEMBIOL.2007.12.013