Magnesium in PDB 1plk: Crystallographic Studies on P21H-Ras Using Synchrotron Laue Method: Improvement of Crystal Quality and Monitoring of the Gtpase Reaction at Different Time Points

The structure of Crystallographic Studies on P21H-Ras Using Synchrotron Laue Method: Improvement of Crystal Quality and Monitoring of the Gtpase Reaction at Different Time Points, PDB code: 1plk was solved by A.Scheidig, A.Sanchez-Llorente, A.Lautwein, E.F.Pai, J.E.T.Corrie, G.P.Reid, A.Wittinghofer, R.S.Goody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	40.300, 40.300, 158.600, 90.00, 90.00, 120.00
R / Rfree (%)	22.8 / n/a

The binding sites of Magnesium atom in the Crystallographic Studies on P21H-Ras Using Synchrotron Laue Method: Improvement of Crystal Quality and Monitoring of the Gtpase Reaction at Different Time Points (pdb code 1plk). 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 Crystallographic Studies on P21H-Ras Using Synchrotron Laue Method: Improvement of Crystal Quality and Monitoring of the Gtpase Reaction at Different Time Points, PDB code: 1plk:

Magnesium binding site 1 out of 1 in the Crystallographic Studies on P21H-Ras Using Synchrotron Laue Method: Improvement of Crystal Quality and Monitoring of the Gtpase Reaction at Different Time Points


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystallographic Studies on P21H-Ras Using Synchrotron Laue Method: Improvement of Crystal Quality and Monitoring of the Gtpase Reaction at Different Time Points within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg168 b:20.0 occ:1.00 O A:THR58 2.2 10.6 1.0 O2B A:GTP167 2.4 20.0 1.0 O2G A:GTP167 2.8 20.0 1.0 N A:SER17 2.8 21.5 1.0 OG A:SER17 2.8 2.0 1.0 CB A:LYS16 3.1 24.8 1.0 PB A:GTP167 3.1 20.0 1.0 O1B A:GTP167 3.1 20.0 1.0 C A:THR58 3.4 10.6 1.0 O3G A:GTP167 3.5 20.0 1.0 CB A:SER17 3.5 2.0 1.0 PG A:GTP167 3.6 20.0 1.0 CA A:SER17 3.6 21.5 1.0 C A:LYS16 3.8 18.2 1.0 CA A:LYS16 3.8 18.2 1.0 O3B A:GTP167 3.8 20.0 1.0 CG A:LYS16 3.9 24.8 1.0 OD1 A:ASP57 3.9 19.1 1.0 CE A:LYS16 4.0 24.8 1.0 N A:LYS16 4.0 18.2 1.0 N A:ALA59 4.2 39.1 1.0 CA A:ALA59 4.2 39.1 1.0 O3A A:GTP167 4.3 20.0 1.0 OD2 A:ASP57 4.4 19.1 1.0 CD A:LYS16 4.5 24.8 1.0 CG A:ASP57 4.5 19.1 1.0 NZ A:LYS16 4.6 24.8 1.0 CA A:THR58 4.6 10.6 1.0 N A:THR58 4.7 10.6 1.0 O1A A:GTP167 4.8 20.0 1.0 O1G A:GTP167 5.0 20.0 1.0 O A:LYS16 5.0 18.2 1.0 CB A:ALA59 5.0 73.4 1.0

A.J.Scheidig, A.Sanchez-Llorente, A.Lautwein, E.F.Pai, J.E.Corrie, G.P.Reid, A.Wittinghofer, R.S.Goody. Crystallographic Studies on P21(H-Ras) Using the Synchrotron Laue Method: Improvement of Crystal Quality and Monitoring of the Gtpase Reaction at Different Time Points. Acta Crystallogr.,Sect.D V. 50 512 1994.
ISSN: ISSN 0907-4449
PubMed: 15299412
DOI: 10.1107/S090744499301443X