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Calcium in PDB 1i2f: Ribonuclease T1 V16A Mutant, Form II

Enzymatic activity of Ribonuclease T1 V16A Mutant, Form II

All present enzymatic activity of Ribonuclease T1 V16A Mutant, Form II:
3.1.27.3;

Protein crystallography data

The structure of Ribonuclease T1 V16A Mutant, Form II, PDB code: 1i2f 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) 15.00 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.393, 42.773, 56.664, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 20.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Ribonuclease T1 V16A Mutant, Form II (pdb code 1i2f). 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 V16A Mutant, Form II, PDB code: 1i2f:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1i2f

Go back to Calcium Binding Sites List in 1i2f
Calcium binding site 1 out of 2 in the Ribonuclease T1 V16A Mutant, Form II


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ribonuclease T1 V16A Mutant, Form II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca106

b:16.8
occ:1.00
O A:HOH111 2.4 11.6 1.0
O A:HOH128 2.5 19.2 1.0
O A:HOH120 2.5 16.8 1.0
OD2 A:ASP15 2.5 9.6 1.0
O A:HOH132 2.6 36.1 1.0
O A:HOH119 2.6 13.2 1.0
OD1 A:ASP15 2.7 10.4 1.0
O A:HOH133 2.8 31.3 1.0
CG A:ASP15 2.9 8.4 1.0
O A:HOH117 4.4 20.8 1.0
CB A:ASP15 4.4 6.2 1.0
O A:HOH126 4.5 15.7 1.0
O A:CYS10 4.7 9.7 1.0
OG A:SER12 4.7 7.2 1.0
O A:HOH114 4.8 14.6 1.0
CA A:GLY65 4.9 14.7 1.0

Calcium binding site 2 out of 2 in 1i2f

Go back to Calcium Binding Sites List in 1i2f
Calcium binding site 2 out of 2 in the Ribonuclease T1 V16A Mutant, Form II


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Ribonuclease T1 V16A Mutant, Form II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca107

b:31.2
occ:1.00
O A:HOH150 2.3 34.7 1.0
OD1 A:ASP66 2.4 14.6 1.0
O A:HOH151 2.4 32.6 1.0
CG A:ASP66 3.4 15.6 1.0
OD2 A:ASP66 3.8 16.4 1.0
O A:SER64 4.4 17.9 1.0
CB A:ASP66 4.7 14.0 1.0
N A:ASP66 4.8 13.3 1.0
CA A:ASP66 4.9 12.6 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: Thu Jul 11 10:14:38 2024

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