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Magnesium in PDB 2rgg: Crystal Structure of H-RASQ61I-Gppnhp, Trigonal Crystal Form

Protein crystallography data

The structure of Crystal Structure of H-RASQ61I-Gppnhp, Trigonal Crystal Form, PDB code: 2rgg was solved by G.Buhrman, G.Wink, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.84 / 1.45
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 39.688, 39.688, 159.015, 90.00, 90.00, 120.00
R / Rfree (%) 21.5 / 23.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of H-RASQ61I-Gppnhp, Trigonal Crystal Form (pdb code 2rgg). 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 H-RASQ61I-Gppnhp, Trigonal Crystal Form, PDB code: 2rgg:

Magnesium binding site 1 out of 1 in 2rgg

Go back to Magnesium Binding Sites List in 2rgg
Magnesium binding site 1 out of 1 in the Crystal Structure of H-RASQ61I-Gppnhp, Trigonal Crystal Form


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 H-RASQ61I-Gppnhp, Trigonal Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:15.1
occ:1.00
OG1 A:THR35 2.0 17.7 1.0
O A:HOH668 2.0 15.7 1.0
OG A:SER17 2.1 14.8 1.0
O A:HOH669 2.1 15.9 1.0
O2G A:GNP528 2.2 17.1 1.0
O2B A:GNP528 2.2 15.7 1.0
CB A:THR35 3.0 18.1 1.0
CB A:SER17 3.1 13.4 1.0
PG A:GNP528 3.2 14.9 1.0
PB A:GNP528 3.3 13.6 1.0
N3B A:GNP528 3.4 14.0 1.0
N A:THR35 3.8 17.6 1.0
N A:SER17 3.8 12.4 1.0
OD2 A:ASP57 3.9 19.0 1.0
CA A:THR35 4.0 18.7 1.0
CA A:SER17 4.0 13.2 1.0
O3G A:GNP528 4.0 17.0 1.0
CG2 A:THR35 4.1 18.3 1.0
OD1 A:ASP57 4.1 18.5 1.0
O A:THR58 4.3 18.9 1.0
O A:HOH612 4.3 22.3 1.0
O1B A:GNP528 4.3 13.4 1.0
O2A A:GNP528 4.3 15.7 1.0
O3A A:GNP528 4.3 13.1 1.0
O1G A:GNP528 4.4 17.3 1.0
CG A:ASP57 4.4 16.4 1.0
O A:ASP33 4.5 19.9 1.0
PA A:GNP528 4.6 14.3 1.0
O1A A:GNP528 4.7 14.7 1.0
C A:PRO34 4.8 19.9 1.0
CB A:LYS16 4.8 13.3 1.0
CE A:LYS16 4.9 14.6 1.0
C A:LYS16 4.9 12.8 1.0

Reference:

G.Buhrman, G.Wink, C.Mattos. Transformation Efficiency of RASQ61 Mutants Linked to Structural Features of the Switch Regions in the Presence of Raf. Structure V. 15 1618 2007.
ISSN: ISSN 0969-2126
PubMed: 18073111
DOI: 10.1016/J.STR.2007.10.011
Page generated: Mon Dec 14 07:38:33 2020

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