Magnesium in PDB 5p21: Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 Angstroms Resolution: Implications For the Mechanism of Gtp Hydrolysis

The structure of Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 Angstroms Resolution: Implications For the Mechanism of Gtp Hydrolysis, PDB code: 5p21 was solved by E.F.Pai, A.Wittinghofer, W.Kabsch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 1.35
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	40.300, 40.300, 162.200, 90.00, 90.00, 120.00
R / Rfree (%)	19.6 / n/a

The binding sites of Magnesium atom in the Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 Angstroms Resolution: Implications For the Mechanism of Gtp Hydrolysis (pdb code 5p21). 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 Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 Angstroms Resolution: Implications For the Mechanism of Gtp Hydrolysis, PDB code: 5p21:

Magnesium binding site 1 out of 1 in the Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 Angstroms Resolution: Implications For the Mechanism of Gtp Hydrolysis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 Angstroms Resolution: Implications For the Mechanism of Gtp Hydrolysis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg168 b:9.4 occ:1.00 O2G A:GNP167 2.2 11.2 1.0 O2B A:GNP167 2.2 9.4 1.0 O A:HOH173 2.2 8.2 1.0 OG A:SER17 2.3 8.8 1.0 OG1 A:THR35 2.3 11.2 1.0 O A:HOH172 2.3 11.3 1.0 CB A:THR35 3.2 11.3 1.0 CB A:SER17 3.2 8.2 1.0 PG A:GNP167 3.2 9.7 1.0 PB A:GNP167 3.3 8.8 1.0 N3B A:GNP167 3.5 8.2 1.0 N A:THR35 3.8 11.0 1.0 N A:SER17 3.9 7.7 1.0 O3G A:GNP167 4.0 10.1 1.0 CA A:SER17 4.1 8.8 1.0 CA A:THR35 4.1 11.5 1.0 OD2 A:ASP57 4.1 13.2 1.0 CG2 A:THR35 4.2 13.1 1.0 O2A A:GNP167 4.2 9.3 1.0 OD1 A:ASP57 4.3 11.1 1.0 O1B A:GNP167 4.3 8.3 1.0 O A:HOH171 4.3 18.3 1.0 O3A A:GNP167 4.3 10.2 1.0 O1G A:GNP167 4.4 9.3 1.0 O A:THR58 4.4 14.0 1.0 O A:ASP33 4.5 12.5 1.0 PA A:GNP167 4.5 10.2 1.0 CG A:ASP57 4.6 11.4 1.0 O1A A:GNP167 4.6 10.1 1.0 C A:PRO34 4.8 11.8 1.0 CB A:LYS16 4.9 9.3 1.0 C A:LYS16 4.9 9.0 1.0 CE A:LYS16 5.0 10.1 1.0

E.F.Pai, U.Krengel, G.A.Petsko, R.S.Goody, W.Kabsch, A.Wittinghofer. Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 A Resolution: Implications For the Mechanism of Gtp Hydrolysis. Embo J. V. 9 2351 1990.
ISSN: ISSN 0261-4189
PubMed: 2196171