Magnesium in PDB 1a2b: Human Rhoa Complexed with Gtp Analogue

The structure of Human Rhoa Complexed with Gtp Analogue, PDB code: 1a2b was solved by K.Ihara, S.Muraguchi, M.Kato, T.Shimizu, M.Shirakawa, S.Kuroda, K.Kaibuchi, T.Hakoshima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.40
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	62.020, 74.780, 50.520, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 26.8

The binding sites of Magnesium atom in the Human Rhoa Complexed with Gtp Analogue (pdb code 1a2b). 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 Human Rhoa Complexed with Gtp Analogue, PDB code: 1a2b:

Magnesium binding site 1 out of 1 in the Human Rhoa Complexed with Gtp Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Rhoa Complexed with Gtp Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg550 b:29.3 occ:1.00 O A:HOH604 1.9 10.9 1.0 O A:HOH605 2.0 27.3 1.0 OG1 A:THR19 2.0 40.3 1.0 OG1 A:THR37 2.1 51.9 1.0 O2G A:GSP538 2.3 31.6 1.0 O2B A:GSP538 2.5 2.0 1.0 CB A:THR19 3.1 30.8 1.0 CB A:THR37 3.2 41.5 1.0 PG A:GSP538 3.5 39.5 1.0 PB A:GSP538 3.6 33.6 1.0 O3B A:GSP538 3.8 44.1 1.0 N A:THR37 3.9 41.6 1.0 OD2 A:ASP59 4.0 22.1 1.0 N A:THR19 4.0 35.6 1.0 CA A:THR19 4.1 34.0 1.0 O2A A:GSP538 4.1 18.9 1.0 CG2 A:THR19 4.2 24.5 1.0 CA A:THR37 4.2 39.6 1.0 O3G A:GSP538 4.3 32.6 1.0 CG2 A:THR37 4.3 46.2 1.0 OD1 A:ASP59 4.3 12.8 1.0 O A:VAL35 4.4 60.3 1.0 O3A A:GSP538 4.5 25.4 1.0 CG A:ASP59 4.5 30.8 1.0 O A:THR60 4.6 31.4 1.0 PA A:GSP538 4.7 20.3 1.0 O1A A:GSP538 4.7 24.6 1.0 O1B A:GSP538 4.8 33.8 1.0 C A:PRO36 4.9 44.0 1.0 CB A:LYS18 4.9 31.3 1.0

K.Ihara, S.Muraguchi, M.Kato, T.Shimizu, M.Shirakawa, S.Kuroda, K.Kaibuchi, T.Hakoshima. Crystal Structure of Human Rhoa in A Dominantly Active Form Complexed with A Gtp Analogue. J.Biol.Chem. V. 273 9656 1998.
ISSN: ISSN 0021-9258
PubMed: 9545299
DOI: 10.1074/JBC.273.16.9656