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Magnesium in PDB 2rga: Crystal Structure of H-RASQ61I-Gppnhp

Protein crystallography data

The structure of Crystal Structure of H-RASQ61I-Gppnhp, PDB code: 2rga 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) 28.26 / 1.90
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 88.342, 88.342, 133.419, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 21.2

Other elements in 2rga:

The structure of Crystal Structure of H-RASQ61I-Gppnhp also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of H-RASQ61I-Gppnhp (pdb code 2rga). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of H-RASQ61I-Gppnhp, PDB code: 2rga:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2rga

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


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:22.6
occ:0.50
O A:HOH688 2.1 17.2 1.0
O A:HOH689 2.1 15.2 1.0
O A:THR124 3.9 18.2 1.0
NE2 A:GLN129 4.1 25.0 1.0
O A:HOH622 4.2 25.0 1.0
OE1 A:GLN129 4.4 22.9 1.0
CD A:GLN129 4.7 23.5 1.0
C A:THR124 5.0 17.3 1.0

Magnesium binding site 2 out of 2 in 2rga

Go back to Magnesium Binding Sites List in 2rga
Magnesium binding site 2 out of 2 in the Crystal Structure of H-RASQ61I-Gppnhp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of H-RASQ61I-Gppnhp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg603

b:15.7
occ:1.00
OG A:SER17 2.1 14.6 1.0
O A:HOH670 2.1 12.9 1.0
O2G A:GNP528 2.2 16.9 1.0
OG1 A:THR35 2.2 14.3 1.0
O A:HOH669 2.2 17.1 1.0
O2B A:GNP528 2.2 12.8 1.0
CB A:THR35 3.0 17.2 1.0
CB A:SER17 3.2 15.5 1.0
PG A:GNP528 3.2 16.8 1.0
PB A:GNP528 3.2 15.3 1.0
N3B A:GNP528 3.4 14.2 1.0
N A:THR35 3.9 16.4 1.0
N A:SER17 3.9 12.6 1.0
O3G A:GNP528 3.9 16.0 1.0
OD2 A:ASP57 4.0 21.8 1.0
CA A:THR35 4.1 16.0 1.0
CA A:SER17 4.1 13.3 1.0
O2A A:GNP528 4.1 13.7 1.0
CG2 A:THR35 4.1 15.1 1.0
O A:HOH649 4.1 19.0 1.0
OD1 A:ASP57 4.2 21.2 1.0
O3A A:GNP528 4.3 12.3 1.0
O1B A:GNP528 4.3 13.1 1.0
O1G A:GNP528 4.4 17.0 1.0
O A:ASP33 4.4 15.3 1.0
CG A:ASP57 4.5 21.1 1.0
O A:THR58 4.5 17.8 1.0
PA A:GNP528 4.5 14.8 1.0
O1A A:GNP528 4.7 13.5 1.0
C A:PRO34 4.8 17.4 1.0
CB A:LYS16 4.8 13.3 1.0
C A:LYS16 4.9 13.3 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 07:38:30 2020

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