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Calcium in PDB 1i2g: Ribonuclease T1 V16T Mutant

Enzymatic activity of Ribonuclease T1 V16T Mutant

All present enzymatic activity of Ribonuclease T1 V16T Mutant:
3.1.27.3;

Protein crystallography data

The structure of Ribonuclease T1 V16T Mutant, PDB code: 1i2g was solved by S.De Vos, J.Backmann, J.Steyaert, R.Loris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.00 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.412, 42.681, 56.695, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 19.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Ribonuclease T1 V16T Mutant (pdb code 1i2g). 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 V16T Mutant, PDB code: 1i2g:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1i2g

Go back to Calcium Binding Sites List in 1i2g
Calcium binding site 1 out of 2 in the Ribonuclease T1 V16T 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 V16T Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca106

b:10.3
occ:1.00
OD2 A:ASP15 2.4 10.9 1.0
O A:HOH111 2.4 7.9 1.0
O A:HOH119 2.4 12.6 1.0
O A:HOH120 2.5 14.2 1.0
O A:HOH133 2.5 21.7 1.0
O A:HOH128 2.5 15.2 1.0
OD1 A:ASP15 2.6 10.1 1.0
O A:HOH136 2.8 22.0 1.0
CG A:ASP15 2.8 9.9 1.0
CB A:ASP15 4.3 9.7 1.0
O A:HOH117 4.4 12.5 1.0
OG A:SER12 4.5 6.6 1.0
O A:CYS10 4.6 7.3 1.0
O A:HOH126 4.7 16.9 1.0
O A:HOH114 4.7 10.6 1.0
N A:SER12 4.9 7.3 1.0
CA A:GLY65 5.0 13.9 1.0
O A:HOH142 5.0 29.8 1.0

Calcium binding site 2 out of 2 in 1i2g

Go back to Calcium Binding Sites List in 1i2g
Calcium binding site 2 out of 2 in the Ribonuclease T1 V16T 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 V16T Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca107

b:24.5
occ:1.00
OD1 A:ASP66 2.6 15.4 1.0
O A:HOH160 2.7 32.6 1.0
CG A:ASP66 3.7 14.3 1.0
OD2 A:ASP66 4.0 16.4 1.0
O A:SER64 4.4 17.6 1.0
CB A:ASP66 5.0 12.3 1.0

Reference:

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
Page generated: Mon Jul 7 15:45:55 2025

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