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Calcium in PDB 3d6c: Crystal Structure of Staphylococcal Nuclease Variant Phs L38E at Cryogenic Temperature

Enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant Phs L38E at Cryogenic Temperature

All present enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant Phs L38E at Cryogenic Temperature:
3.1.31.1;

Protein crystallography data

The structure of Crystal Structure of Staphylococcal Nuclease Variant Phs L38E at Cryogenic Temperature, PDB code: 3d6c was solved by M.J.Harms, J.L.Schlessman, G.R.Sue, E.B.Garcia-Moreno, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.28 / 2.00
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 48.256, 48.256, 62.675, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 23.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Staphylococcal Nuclease Variant Phs L38E at Cryogenic Temperature (pdb code 3d6c). 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 Phs L38E at Cryogenic Temperature, PDB code: 3d6c:

Calcium binding site 1 out of 1 in 3d6c

Go back to Calcium Binding Sites List in 3d6c
Calcium binding site 1 out of 1 in the Crystal Structure of Staphylococcal Nuclease Variant Phs L38E 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 Phs L38E at Cryogenic Temperature within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca150

b:17.7
occ:1.00
OD1 A:ASP40 2.3 14.1 1.0
OD2 A:ASP21 2.5 10.5 1.0
O A:HOH212 2.5 16.1 1.0
O6P A:THP151 2.6 14.2 1.0
O A:HOH213 2.7 12.0 1.0
O A:HOH176 2.7 11.3 1.0
O A:THR41 2.8 16.9 1.0
CG A:ASP21 3.3 9.9 1.0
OD1 A:ASP21 3.4 10.3 1.0
CG A:ASP40 3.5 14.2 1.0
P2 A:THP151 3.8 18.9 1.0
NH1 A:ARG35 3.8 11.0 1.0
C A:THR41 3.8 15.6 1.0
N A:THR41 3.8 13.3 1.0
O A:HOH169 3.9 15.7 1.0
O5P A:THP151 4.0 12.0 1.0
OG1 A:THR41 4.0 14.1 1.0
OD2 A:ASP40 4.2 15.5 1.0
CA A:THR41 4.4 14.4 1.0
CZ A:ARG35 4.4 12.0 1.0
C A:ASP40 4.5 13.4 1.0
O4P A:THP151 4.5 17.9 1.0
CA A:ASP40 4.5 13.8 1.0
O A:HOH243 4.5 26.8 1.0
NE A:ARG35 4.5 10.1 1.0
OE1 A:GLU43 4.5 21.9 1.0
OD2 A:ASP19 4.6 13.1 1.0
CB A:ASP40 4.6 14.0 1.0
CB A:ASP21 4.7 8.7 1.0
C A:PRO42 4.8 19.9 1.0
O A:PRO42 4.8 20.5 1.0
CB A:THR41 4.9 13.7 1.0
N A:PRO42 4.9 17.6 1.0
O5' A:THP151 5.0 16.1 1.0

Reference:

M.J.Harms, C.A.Castaneda, J.L.Schlessman, G.R.Sue, D.G.Isom, B.R.Cannon, E.B.Garcia-Moreno. The Pk(A) Values of Acidic and Basic Residues Buried at the Same Internal Location in A Protein Are Governed By Different Factors. J.Mol.Biol. V. 389 34 2009.
ISSN: ISSN 0022-2836
PubMed: 19324049
DOI: 10.1016/J.JMB.2009.03.039
Page generated: Sat Jul 13 08:53:07 2024

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