Magnesium in PDB 1n6l: Crystal Structure of Human RAB5A A30P Mutant Complex with Gtp

The structure of Crystal Structure of Human RAB5A A30P Mutant Complex with Gtp, PDB code: 1n6l was solved by G.Zhu, J.Liu, S.Terzyan, P.Zhai, G.Li, X.C.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	35.750, 64.200, 65.860, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 21.1

The binding sites of Magnesium atom in the Crystal Structure of Human RAB5A A30P Mutant Complex with Gtp (pdb code 1n6l). 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 Human RAB5A A30P Mutant Complex with Gtp, PDB code: 1n6l:

Magnesium binding site 1 out of 1 in the Crystal Structure of Human RAB5A A30P Mutant Complex with Gtp


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 Human RAB5A A30P Mutant Complex with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:8.9 occ:1.00 O2G A:GTP200 2.0 11.1 1.0 O2B A:GTP200 2.1 7.1 1.0 O A:HOH301 2.1 8.6 1.0 OG1 A:THR52 2.1 8.1 1.0 OG A:SER34 2.1 8.6 1.0 O A:HOH302 2.1 8.7 1.0 CB A:THR52 3.2 12.8 1.0 PG A:GTP200 3.2 10.3 1.0 CB A:SER34 3.2 8.0 1.0 PB A:GTP200 3.2 8.4 1.0 O3B A:GTP200 3.4 9.9 1.0 N A:THR52 3.8 12.6 1.0 N A:SER34 3.9 7.9 1.0 O3G A:GTP200 3.9 11.7 1.0 CA A:THR52 4.1 11.2 1.0 OD2 A:ASP75 4.1 9.9 1.0 O2A A:GTP200 4.1 10.3 1.0 CA A:SER34 4.1 8.7 1.0 O A:HOH312 4.2 14.1 1.0 OD1 A:ASP75 4.2 9.6 1.0 CG2 A:THR52 4.3 12.7 1.0 O3A A:GTP200 4.3 8.1 1.0 O1B A:GTP200 4.3 8.2 1.0 O1G A:GTP200 4.4 11.8 1.0 CG A:ASP75 4.5 10.1 1.0 PA A:GTP200 4.6 8.5 1.0 O A:THR76 4.6 11.6 1.0 O1A A:GTP200 4.6 7.9 1.0 O A:GLU50 4.7 13.9 1.0 C A:SER51 4.8 15.7 1.0 CB A:LYS33 4.9 8.5 1.0

G.Zhu, J.Liu, S.Terzyan, P.Zhai, G.Li, X.C.Zhang. High Resolution Crystal Structures of Human RAB5A and Five Mutants with Substitutions in the Catalytically Important Phosphate-Binding Loop J.Biol.Chem. V. 278 2452 2003.
ISSN: ISSN 0021-9258
PubMed: 12433916
DOI: 10.1074/JBC.M211042200