Calcium in PDB 1fys: Ribonuclease T1 V16C Mutant

All present enzymatic activity of Ribonuclease T1 V16C Mutant:
3.1.27.3;

The structure of Ribonuclease T1 V16C Mutant, PDB code: 1fys was solved by S.De Vos, R.Loris, J.Steyaert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	2.09 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.445, 42.679, 56.651, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 20.8

The binding sites of Calcium atom in the Ribonuclease T1 V16C Mutant (pdb code 1fys). 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 V16C Mutant, PDB code: 1fys:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Ribonuclease T1 V16C Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ribonuclease T1 V16C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca106 b:13.6 occ:1.00 O A:HOH128 2.4 19.4 1.0 O A:HOH174 2.4 31.8 1.0 O A:HOH119 2.5 11.6 1.0 O A:HOH111 2.5 12.0 1.0 OD2 A:ASP15 2.5 14.6 1.0 O A:HOH120 2.6 21.9 1.0 OD1 A:ASP15 2.7 16.1 1.0 CG A:ASP15 3.0 12.8 1.0 O A:HOH132 3.0 42.1 1.0 O A:HOH117 4.4 18.5 1.0 CB A:ASP15 4.5 10.3 1.0 OG A:SER12 4.5 9.7 1.0 O A:HOH126 4.5 17.4 1.0 O A:CYS10 4.7 12.8 1.0 O A:HOH114 4.8 17.4 1.0 O A:HOH163 4.9 30.5 1.0

Calcium binding site 2 out of 2 in the Ribonuclease T1 V16C Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Ribonuclease T1 V16C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca107 b:31.3 occ:1.00 OD1 A:ASP66 2.5 17.1 1.0 CG A:ASP66 3.6 16.6 1.0 OD2 A:ASP66 3.9 18.3 1.0 O A:SER64 4.5 21.4 1.0 CB A:ASP66 4.9 14.4 1.0

S.De Vos, J.Backmann, M.Prevost, J.Steyaert, R.Loris. Hydrophobic Core Manipulations in Ribonuclease T1. Biochemistry V. 40 10140 2001.
ISSN: ISSN 0006-2960
PubMed: 11513591
DOI: 10.1021/BI010565N