Calcium in PDB 8els: Hras R97A Crystal Form 1 R-State

All present enzymatic activity of Hras R97A Crystal Form 1 R-State:
3.6.5.2;

The structure of Hras R97A Crystal Form 1 R-State, PDB code: 8els was solved by D.Davis, C.W.Johnson, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.71 / 2.27
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	88.856, 88.856, 134.953, 90, 90, 120
R / Rfree (%)	16.2 / 21.2

The structure of Hras R97A Crystal Form 1 R-State also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Calcium atom in the Hras R97A Crystal Form 1 R-State (pdb code 8els). 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 R97A Crystal Form 1 R-State, PDB code: 8els:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Hras R97A Crystal Form 1 R-State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Hras R97A Crystal Form 1 R-State within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca202 b:29.0 occ:1.00 O A:PHE28 2.2 29.6 1.0 OD1 A:ASP30 2.3 30.4 1.0 C A:PHE28 3.4 23.4 1.0 CG A:ASP30 3.5 24.8 1.0 N A:ASP30 4.0 26.1 1.0 O A:HOH346 4.2 33.6 1.0 CA A:VAL29 4.2 20.6 1.0 N A:VAL29 4.3 26.6 1.0 OD2 A:ASP30 4.4 32.5 1.0 CB A:ASP30 4.4 26.0 1.0 CA A:PHE28 4.4 22.0 1.0 N A:PHE28 4.6 25.5 1.0 C A:VAL29 4.6 25.7 1.0 CB A:PHE28 4.7 24.6 1.0 CA A:ASP30 4.8 28.9 1.0 ND1 A:HIS27 4.9 28.4 1.0 CD2 A:PHE28 5.0 27.5 1.0

Calcium binding site 2 out of 2 in the Hras R97A Crystal Form 1 R-State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Hras R97A Crystal Form 1 R-State within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca204 b:55.5 occ:0.33 O A:HOH376 2.3 40.6 1.0 O A:HOH325 2.4 38.1 1.0 O A:HOH302 4.0 39.3 1.0 NE2 A:GLN129 4.1 44.1 1.0 O A:THR124 4.2 33.7 1.0 OE1 A:GLN129 4.4 33.8 1.0 CD A:GLN129 4.7 45.7 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