Calcium in PDB 8elt: Hras R97G Crystal Form 2

All present enzymatic activity of Hras R97G Crystal Form 2:
3.6.5.2;

The structure of Hras R97G Crystal Form 2, PDB code: 8elt was solved by C.W.Johnson, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.72 / 1.66
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	38.941, 38.941, 157.386, 90, 90, 120
R / Rfree (%)	19.8 / 23.9

The structure of Hras R97G Crystal Form 2 also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Calcium atom in the Hras R97G Crystal Form 2 (pdb code 8elt). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Hras R97G Crystal Form 2, PDB code: 8elt:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Hras R97G Crystal Form 2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Hras R97G Crystal Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca204 b:52.8 occ:1.00 OE2 A:GLU162 2.4 31.6 1.0 O A:HOH392 2.4 40.6 1.0 O A:HOH423 2.4 40.0 0.7 OE1 A:GLU162 2.5 27.3 1.0 O A:HOH343 2.5 37.6 1.0 O A:HOH401 2.6 52.8 1.0 O A:HOH363 2.6 45.4 1.0 CD A:GLU162 2.8 29.0 1.0 O A:HOH408 3.9 51.0 1.0 CG A:GLU162 4.3 25.9 1.0 O A:HOH390 4.3 41.6 1.0 O A:HOH411 4.5 37.0 0.5 NE2 A:GLN165 4.6 40.0 1.0 O A:HOH323 4.8 25.5 1.0 CG A:PRO140 4.8 25.7 1.0 CD A:PRO140 4.8 26.2 1.0 O A:GLY138 4.9 31.2 1.0

Calcium binding site 2 out of 2 in the Hras R97G Crystal Form 2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Hras R97G Crystal Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca205 b:34.1 occ:1.00 OD1 A:ASP108 2.4 38.1 1.0 O A:HOH394 2.4 37.7 1.0 OD1 A:ASP107 2.4 31.1 1.0 OD2 A:ASP108 2.5 36.9 1.0 O A:HOH397 2.6 41.3 1.0 CG A:ASP108 2.8 36.2 1.0 CG A:ASP107 3.6 34.5 1.0 O A:HOH380 3.9 44.5 1.0 OD2 A:ASP107 4.0 34.5 1.0 CB A:ASP108 4.2 32.2 1.0 C A:ASP107 4.5 30.4 1.0 O A:HOH312 4.5 47.8 1.0 N A:ASP108 4.6 28.5 1.0 O A:ASP107 4.7 29.7 1.0 CB A:ASP107 4.8 37.0 1.0 CA A:ASP108 4.8 34.0 1.0 N A:ASP107 4.9 28.3 1.0 CA A:ASP107 5.0 30.8 1.0

C.W.Johnson, S.K.Fetics, K.P.Davis, J.A.Rodrigues, C.Mattos. Allosteric Site Variants Affect Gtp Hydrolysis on Ras. Protein Sci. E4767 2023.
ISSN: ESSN 1469-896X
PubMed: 37615343
DOI: 10.1002/PRO.4767