Calcium in PDB 8elv: Hras R97I Crystal Form 2

All present enzymatic activity of Hras R97I Crystal Form 2:
3.6.5.2;

The structure of Hras R97I Crystal Form 2, PDB code: 8elv 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)	33.77 / 2.15
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	38.999, 38.999, 158.077, 90, 90, 120
R / Rfree (%)	18.4 / 27

The structure of Hras R97I Crystal Form 2 also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Calcium atom in the Hras R97I Crystal Form 2 (pdb code 8elv). 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 R97I Crystal Form 2, PDB code: 8elv:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Hras R97I 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 R97I Crystal Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca203 b:47.1 occ:1.00 OD1 A:ASP105 2.4 44.2 1.0 O A:HOH325 2.5 33.3 1.0 O A:ARG102 2.8 38.7 1.0 CG A:ASP105 3.4 27.3 1.0 OD2 A:ASP105 3.7 37.2 1.0 C A:ARG102 3.9 38.9 1.0 CA A:ARG102 4.4 37.6 1.0 CB A:ASP105 4.7 31.9 1.0 CB A:ARG102 4.8 28.4 1.0 CA A:ASP105 4.9 30.5 1.0 N A:VAL103 5.0 27.0 1.0

Calcium binding site 2 out of 2 in the Hras R97I 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 R97I Crystal Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca204 b:43.2 occ:1.00 OD1 A:ASP108 2.6 35.0 0.4 OD1 A:ASP107 2.7 40.5 1.0 O A:HOH370 2.9 37.4 1.0 CG A:ASP108 3.3 36.8 0.4 CG A:ASP107 3.9 38.8 1.0 OD1 A:ASP108 3.9 39.6 0.6 CG A:ASP108 3.9 37.4 0.6 CB A:ASP108 4.0 35.8 0.6 CB A:ASP108 4.0 35.9 0.4 OD2 A:ASP108 4.0 36.8 0.4 N A:ASP108 4.3 26.4 1.0 OD2 A:ASP108 4.5 39.8 0.6 OD2 A:ASP107 4.5 34.0 1.0 C A:ASP107 4.6 27.4 1.0 CA A:ASP108 4.7 37.1 0.4 CA A:ASP108 4.8 36.6 0.6 N A:ASP107 4.8 29.7 1.0 CB A:ASP107 4.9 37.2 1.0 O A:ASP107 4.9 33.3 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