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Calcium in PDB 3oiv: H-RASG12V with Allosteric Switch in the "Off" State

Protein crystallography data

The structure of H-RASG12V with Allosteric Switch in the "Off" State, PDB code: 3oiv was solved by G.Buhrman, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.40 / 1.84
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 87.883, 87.883, 133.057, 90.00, 90.00, 120.00
R / Rfree (%) 15.8 / 19.8

Other elements in 3oiv:

The structure of H-RASG12V with Allosteric Switch in the "Off" State also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the H-RASG12V with Allosteric Switch in the "Off" State (pdb code 3oiv). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the H-RASG12V with Allosteric Switch in the "Off" State, PDB code: 3oiv:

Calcium binding site 1 out of 1 in 3oiv

Go back to Calcium Binding Sites List in 3oiv
Calcium binding site 1 out of 1 in the H-RASG12V with Allosteric Switch in the "Off" State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of H-RASG12V with Allosteric Switch in the "Off" State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca167

b:13.5
occ:1.00
O A:PHE28 2.4 12.1 1.0
OD2 A:ASP30 2.4 16.1 1.0
O A:HOH200 2.5 16.8 1.0
C A:PHE28 3.6 14.4 1.0
CG A:ASP30 3.7 20.6 1.0
N A:ASP30 4.0 11.8 1.0
CA A:VAL29 4.4 11.0 1.0
N A:VAL29 4.4 10.0 1.0
CB A:ASP30 4.4 18.1 1.0
O A:HOH275 4.4 30.4 1.0
CA A:PHE28 4.5 9.7 1.0
OD1 A:ASP30 4.6 21.3 1.0
N A:PHE28 4.6 11.2 1.0
O A:HOH240 4.6 17.4 1.0
C A:VAL29 4.7 13.5 1.0
CB A:PHE28 4.8 12.8 1.0
CA A:ASP30 4.9 11.6 1.0
ND1 A:HIS27 4.9 13.8 1.0
CD2 A:PHE28 5.0 15.1 1.0

Reference:

G.Buhrman, V.S.Kumar, M.Cirit, J.M.Haugh, C.Mattos. Allosteric Modulation of Ras-Gtp Is Linked to Signal Transduction Through Raf Kinase. J.Biol.Chem. V. 286 3323 2011.
ISSN: ISSN 0021-9258
PubMed: 21098031
DOI: 10.1074/JBC.M110.193854
Page generated: Sat Dec 12 04:23:13 2020

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