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Calcium in PDB 3nhh: Crystal Structure of Staphylococcal Nuclease Variant V23E-L36K at Cryogenic Temperature

Enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant V23E-L36K at Cryogenic Temperature

All present enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant V23E-L36K at Cryogenic Temperature:
3.1.31.1;

Protein crystallography data

The structure of Crystal Structure of Staphylococcal Nuclease Variant V23E-L36K at Cryogenic Temperature, PDB code: 3nhh was solved by A.C.Robinson, J.L.Schlessman, E.B.Garcia-Moreno, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.46 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 31.261, 60.121, 38.567, 90.00, 94.30, 90.00
R / Rfree (%) 19.1 / 25.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Staphylococcal Nuclease Variant V23E-L36K at Cryogenic Temperature (pdb code 3nhh). 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 Crystal Structure of Staphylococcal Nuclease Variant V23E-L36K at Cryogenic Temperature, PDB code: 3nhh:

Calcium binding site 1 out of 1 in 3nhh

Go back to Calcium Binding Sites List in 3nhh
Calcium binding site 1 out of 1 in the Crystal Structure of Staphylococcal Nuclease Variant V23E-L36K at Cryogenic Temperature


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Staphylococcal Nuclease Variant V23E-L36K at Cryogenic Temperature within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca151

b:38.0
occ:1.00
OD1 A:ASP21 2.1 19.7 1.0
O A:THR41 2.4 19.2 1.0
O A:HOH225 2.5 22.2 1.0
OE2 A:GLU43 2.6 48.9 1.0
OD1 A:ASP40 2.7 19.2 1.0
CG A:ASP21 3.2 20.0 1.0
CD A:GLU43 3.6 46.9 1.0
OD2 A:ASP21 3.6 17.6 1.0
C A:THR41 3.6 19.7 1.0
O A:HOH45 3.6 18.1 1.0
CG A:ASP40 3.8 20.9 1.0
CG A:GLU43 3.8 39.2 1.0
N A:THR41 3.9 17.3 1.0
O5P A:THP150 4.0 20.4 1.0
OG1 A:THR41 4.0 17.3 1.0
N A:GLU43 4.3 30.1 1.0
CA A:THR41 4.3 18.4 1.0
C A:PRO42 4.4 25.9 1.0
OD2 A:ASP40 4.4 24.6 1.0
CB A:ASP21 4.5 14.9 1.0
N A:PRO42 4.6 20.8 1.0
C A:ASP40 4.6 16.4 1.0
NH2 A:ARG35 4.6 12.6 1.0
O A:HOH196 4.7 23.2 1.0
OE1 A:GLU43 4.7 49.6 1.0
O A:PRO42 4.7 25.1 1.0
CA A:GLU43 4.8 34.5 1.0
CA A:PRO42 4.8 23.7 1.0
CA A:ASP40 4.8 14.7 1.0
CB A:THR41 4.8 19.0 1.0
P2 A:THP150 4.9 17.7 1.0
CB A:GLU43 4.9 35.3 1.0
CB A:ASP40 4.9 15.0 1.0

Reference:

A.C.Robinson, C.A.Castaneda, J.L.Schlessman, B.Garcia-Moreno E. Structural and Thermodynamic Consequences of Burial of An Artificial Ion Pair in the Hydrophobic Interior of A Protein. Proc.Natl.Acad.Sci.Usa V. 111 11685 2014.
ISSN: ISSN 0027-8424
PubMed: 25074910
DOI: 10.1073/PNAS.1402900111
Page generated: Sat Jul 13 14:59:59 2024

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