Magnesium in PDB 1ky2: Gppnhp-Bound YPT7P at 1.6 A Resolution

The structure of Gppnhp-Bound YPT7P at 1.6 A Resolution, PDB code: 1ky2 was solved by A.-T.Constantinescu, A.Rak, A.J.Scheidig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.137, 60.667, 73.537, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 24.9

The binding sites of Magnesium atom in the Gppnhp-Bound YPT7P at 1.6 A Resolution (pdb code 1ky2). 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 Gppnhp-Bound YPT7P at 1.6 A Resolution, PDB code: 1ky2:

Magnesium binding site 1 out of 1 in the Gppnhp-Bound YPT7P at 1.6 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Gppnhp-Bound YPT7P at 1.6 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:10.9 occ:1.00 O1G A:GNP400 2.0 10.6 1.0 O2B A:GNP400 2.1 9.5 1.0 O A:HOH1008 2.1 12.2 1.0 OG1 A:THR22 2.1 11.7 1.0 OG1 A:THR40 2.2 9.6 1.0 O A:HOH1009 2.2 11.3 1.0 CB A:THR40 3.1 12.4 1.0 PG A:GNP400 3.2 11.9 1.0 CB A:THR22 3.2 11.9 1.0 PB A:GNP400 3.2 10.4 1.0 N3B A:GNP400 3.5 8.9 1.0 N A:THR40 3.7 10.4 1.0 N A:THR22 3.8 8.3 1.0 O2G A:GNP400 3.9 11.9 1.0 CA A:THR40 4.0 11.3 1.0 OD2 A:ASP64 4.0 13.8 1.0 CA A:THR22 4.1 8.6 1.0 O2A A:GNP400 4.1 12.4 1.0 OD1 A:ASP64 4.2 12.9 1.0 CG2 A:THR40 4.2 12.3 1.0 CG2 A:THR22 4.3 11.2 1.0 O3A A:GNP400 4.3 9.5 1.0 O1B A:GNP400 4.3 9.7 1.0 O3G A:GNP400 4.4 14.1 1.0 O A:THR65 4.4 12.9 1.0 O A:HOH1002 4.4 18.6 1.0 O A:LYS38 4.5 16.6 1.0 CG A:ASP64 4.5 14.9 1.0 PA A:GNP400 4.6 12.5 1.0 C A:ALA39 4.6 14.6 1.0 O1A A:GNP400 4.8 11.7 1.0 CA A:ALA39 4.9 13.7 1.0 C A:LYS21 5.0 11.4 1.0 CB A:LYS21 5.0 11.4 1.0

A.T.Constantinescu, A.Rak, K.Alexandrov, H.Esters, R.S.Goody, A.J.Scheidig. Rab-Subfamily-Specific Regions of YPT7P Are Structurally Different From Other Rabgtpases. Structure V. 10 569 2002.
ISSN: ISSN 0969-2126
PubMed: 11937061
DOI: 10.1016/S0969-2126(02)00737-2