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Calcium in PDB 2snm: In A Staphylococcal Nuclease Mutant the Side-Chain of A Lysine Replacing Valine 66 Is Fully Buried in the Hydrophobic Core

Enzymatic activity of In A Staphylococcal Nuclease Mutant the Side-Chain of A Lysine Replacing Valine 66 Is Fully Buried in the Hydrophobic Core

All present enzymatic activity of In A Staphylococcal Nuclease Mutant the Side-Chain of A Lysine Replacing Valine 66 Is Fully Buried in the Hydrophobic Core:
3.1.31.1;

Protein crystallography data

The structure of In A Staphylococcal Nuclease Mutant the Side-Chain of A Lysine Replacing Valine 66 Is Fully Buried in the Hydrophobic Core, PDB code: 2snm was solved by W.E.Stites, A.G.Gittis, E.E.Lattman, D.Shortle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.37 / 1.97
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 47.156, 47.156, 62.020, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the In A Staphylococcal Nuclease Mutant the Side-Chain of A Lysine Replacing Valine 66 Is Fully Buried in the Hydrophobic Core (pdb code 2snm). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the In A Staphylococcal Nuclease Mutant the Side-Chain of A Lysine Replacing Valine 66 Is Fully Buried in the Hydrophobic Core, PDB code: 2snm:

Calcium binding site 1 out of 1 in 2snm

Go back to Calcium Binding Sites List in 2snm
Calcium binding site 1 out of 1 in the In A Staphylococcal Nuclease Mutant the Side-Chain of A Lysine Replacing Valine 66 Is Fully Buried in the Hydrophobic Core


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of In A Staphylococcal Nuclease Mutant the Side-Chain of A Lysine Replacing Valine 66 Is Fully Buried in the Hydrophobic Core within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca150

b:21.8
occ:1.00
 OD1 A:ASP40 2.2 19.2 1.0
OD2 A:ASP21 2.2 13.6 1.0
O A:HOH180 2.3 21.3 1.0
O A:HOH181 2.5 28.9 1.0
O5P A:THP151 2.6 22.3 1.0
O A:HOH155 2.6 19.1 0.9
O A:THR41 2.7 22.1 1.0
CG A:ASP21 3.1 13.4 1.0
CG A:ASP40 3.4 19.8 1.0
OD1 A:ASP21 3.4 13.2 1.0
N A:THR41 3.7 19.8 1.0
NH2 A:ARG35 3.7 14.2 1.0
P2 A:THP151 3.8 21.9 1.0
O A:HOH162 3.8 26.1 1.0
C A:THR41 3.8 21.8 1.0
OG1 A:THR41 3.9 19.7 1.0
O6P A:THP151 4.0 21.8 1.0
OD2 A:ASP40 4.1 20.7 1.0
CA A:ASP40 4.3 18.4 1.0
CZ A:ARG35 4.3 14.1 1.0
C A:ASP40 4.4 18.8 1.0
CA A:THR41 4.4 20.5 1.0
O4P A:THP151 4.4 22.6 1.0
CB A:ASP40 4.5 18.9 1.0
OE1 A:GLU43 4.5 32.8 1.0
NE A:ARG35 4.5 14.0 1.0
CB A:ASP21 4.5 13.7 1.0
OD2 A:ASP19 4.7 21.3 1.0
C A:PRO42 4.8 25.2 1.0
N A:GLU43 4.9 27.1 1.0
CB A:THR41 4.9 20.2 1.0
O A:PRO42 4.9 24.1 1.0
N A:PRO42 4.9 22.9 1.0

Reference:

W.E.Stites, A.G.Gittis, E.E.Lattman, D.Shortle. In A Staphylococcal Nuclease Mutant the Side-Chain of A Lysine Replacing Valine 66 Is Fully Buried in the Hydrophobic Core. J.Mol.Biol. V. 221 7 1991.
ISSN: ISSN 0022-2836
PubMed: 1920420
DOI: 10.1016/0022-2836(91)80195-Z
Page generated: Fri Jul 12 16:07:39 2024

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