Calcium in PDB 4hoh: Ribonuclease T1 (THR93ALA Mutant) Complexed with 2'Gmp

All present enzymatic activity of Ribonuclease T1 (THR93ALA Mutant) Complexed with 2'Gmp:
3.1.27.3;

The structure of Ribonuclease T1 (THR93ALA Mutant) Complexed with 2'Gmp, PDB code: 4hoh was solved by U.Langhorst, R.Loris, V.P.Denisov, J.Doumen, P.Roose, D.Maes, B.Halle, J.Steyaert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.320, 60.310, 101.030, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 23.4

The binding sites of Calcium atom in the Ribonuclease T1 (THR93ALA Mutant) Complexed with 2'Gmp (pdb code 4hoh). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Ribonuclease T1 (THR93ALA Mutant) Complexed with 2'Gmp, PDB code: 4hoh:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Ribonuclease T1 (THR93ALA Mutant) Complexed with 2'Gmp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ribonuclease T1 (THR93ALA Mutant) Complexed with 2'Gmp within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca105 b:17.6 occ:1.00 O C:GLY47 2.3 17.8 1.0 OD1 C:ASP49 2.4 21.1 1.0 CG C:ASP49 3.4 25.7 1.0 C C:GLY47 3.5 18.1 1.0 OD2 C:ASP49 3.8 36.6 1.0 CA C:GLY47 4.2 15.7 1.0 N C:ASP49 4.4 15.0 1.0 C C:PHE48 4.4 16.5 1.0 N C:PHE48 4.5 16.7 1.0 CA C:PHE48 4.6 16.3 1.0 CB C:ASP49 4.7 20.8 1.0 O C:HOH1084 4.8 30.2 1.0 CA C:ASP49 4.8 16.4 1.0 O C:PHE48 4.8 15.9 1.0

Calcium binding site 2 out of 2 in the Ribonuclease T1 (THR93ALA Mutant) Complexed with 2'Gmp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Ribonuclease T1 (THR93ALA Mutant) Complexed with 2'Gmp within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca106 b:28.5 occ:1.00 O D:GLY47 2.3 10.8 1.0 OD1 D:ASP49 2.4 20.1 1.0 CG D:ASP49 3.4 26.4 1.0 C D:GLY47 3.4 16.6 1.0 OD2 D:ASP49 3.6 38.1 1.0 CA D:GLY47 4.1 15.5 1.0 N D:PHE48 4.5 16.1 1.0 N D:ASP49 4.6 18.1 1.0 C D:PHE48 4.6 16.2 1.0 CB D:ASP49 4.8 24.3 1.0 CA D:PHE48 4.8 15.9 1.0 O D:GLU46 5.0 15.2 1.0

U.Langhorst, R.Loris, V.P.Denisov, J.Doumen, P.Roose, D.Maes, B.Halle, J.Steyaert. Dissection of the Structural and Functional Role of A Conserved Hydration Site in Rnase T1. Protein Sci. V. 8 722 1999.
ISSN: ISSN 0961-8368
PubMed: 10211818