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Magnesium in PDB 1qra: Structure of P21RAS in Complex with Gtp at 100 K

Protein crystallography data

The structure of Structure of P21RAS in Complex with Gtp at 100 K, PDB code: 1qra was solved by A.Scheidig, C.Burmester, R.S.Goody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.60
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 39.567, 39.567, 159.255, 90.00, 90.00, 120.00
R / Rfree (%) 16.7 / 22.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of P21RAS in Complex with Gtp at 100 K (pdb code 1qra). 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 Structure of P21RAS in Complex with Gtp at 100 K, PDB code: 1qra:

Magnesium binding site 1 out of 1 in 1qra

Go back to Magnesium Binding Sites List in 1qra
Magnesium binding site 1 out of 1 in the Structure of P21RAS in Complex with Gtp at 100 K


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of P21RAS in Complex with Gtp at 100 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg168

b:12.9
occ:1.00
O2G A:GTP167 1.9 16.6 1.0
O A:HOH1004 2.0 14.2 1.0
OG A:SER17 2.1 13.0 1.0
O2B A:GTP167 2.1 13.2 1.0
OG1 A:THR35 2.1 17.9 1.0
O A:HOH1003 2.1 14.2 1.0
CB A:THR35 3.0 17.1 1.0
CB A:SER17 3.1 12.3 1.0
PG A:GTP167 3.2 15.1 1.0
PB A:GTP167 3.3 12.7 1.0
O3B A:GTP167 3.4 12.9 1.0
N A:THR35 3.7 14.4 1.0
N A:SER17 3.8 12.3 1.0
CA A:THR35 4.0 15.0 1.0
CA A:SER17 4.1 11.9 1.0
O3G A:GTP167 4.1 16.6 1.0
OD2 A:ASP57 4.1 15.8 1.0
CG2 A:THR35 4.1 18.9 1.0
OD1 A:ASP57 4.1 14.8 1.0
O A:HOH1002 4.1 21.2 1.0
O2A A:GTP167 4.2 14.2 1.0
O3A A:GTP167 4.2 12.2 1.0
O1G A:GTP167 4.3 14.5 1.0
O1B A:GTP167 4.4 11.9 1.0
O A:THR58 4.4 19.0 1.0
O A:ASP33 4.4 17.9 1.0
CG A:ASP57 4.4 17.1 1.0
PA A:GTP167 4.5 14.2 1.0
O1A A:GTP167 4.7 13.5 1.0
C A:PRO34 4.7 18.1 1.0
CB A:LYS16 4.8 10.5 1.0
C A:LYS16 4.9 11.8 1.0
CE A:LYS16 5.0 14.0 1.0
CA A:PRO34 5.0 18.3 1.0

Reference:

A.J.Scheidig, C.Burmester, R.S.Goody. The Pre-Hydrolysis State of P21(Ras) in Complex with Gtp: New Insights Into the Role of Water Molecules in the Gtp Hydrolysis Reaction of Ras-Like Proteins. Structure Fold.Des. V. 7 1311 1999.
ISSN: ISSN 0969-2126
PubMed: 10574788
DOI: 10.1016/S0969-2126(00)80021-0
Page generated: Tue Aug 13 11:55:08 2024

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