Calcium in PDB 3erq: Crystal Structure of Staphylococcal Nuclease Variant L25K at Cryogenic Temperature

All present enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant L25K at Cryogenic Temperature:
3.1.31.1;

The structure of Crystal Structure of Staphylococcal Nuclease Variant L25K at Cryogenic Temperature, PDB code: 3erq 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)	23.29 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	30.978, 60.282, 37.961, 90.00, 93.43, 90.00
R / Rfree (%)	20.9 / 27.8

The binding sites of Calcium atom in the Crystal Structure of Staphylococcal Nuclease Variant L25K at Cryogenic Temperature (pdb code 3erq). 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 L25K at Cryogenic Temperature, PDB code: 3erq:

Calcium binding site 1 out of 1 in the Crystal Structure of Staphylococcal Nuclease Variant L25K 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 L25K at Cryogenic Temperature within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca151 b:27.8 occ:1.00 OD1 A:ASP40 2.7 25.9 1.0 O A:THR41 2.7 23.3 1.0 O A:HOH166 2.7 30.4 1.0 O A:HOH178 2.7 30.8 1.0 OD2 A:ASP21 2.9 19.1 1.0 OE2 A:GLU43 3.0 46.2 1.0 O4P A:THP150 3.2 28.2 1.0 O A:HOH192 3.3 40.1 1.0 CG A:ASP21 3.7 21.7 1.0 O A:HOH158 3.8 28.5 1.0 OD1 A:ASP21 3.8 19.7 1.0 C A:THR41 3.8 24.5 1.0 CG A:ASP40 3.9 26.5 1.0 CD A:GLU43 3.9 44.8 1.0 N A:THR41 4.0 23.0 1.0 OG1 A:THR41 4.0 19.8 1.0 NH2 A:ARG35 4.1 16.1 1.0 P2 A:THP150 4.2 29.2 1.0 O5P A:THP150 4.3 26.3 1.0 OE1 A:GLU43 4.3 44.8 1.0 CA A:THR41 4.4 23.3 1.0 O A:HOH167 4.5 39.3 1.0 C A:ASP40 4.6 22.2 1.0 OD2 A:ASP40 4.6 25.6 1.0 CA A:ASP40 4.6 22.2 1.0 CZ A:ARG35 4.7 18.8 1.0 C A:PRO42 4.7 30.0 1.0 O6P A:THP150 4.8 30.9 1.0 CB A:THR41 4.9 23.8 1.0 CB A:ASP40 4.9 21.5 1.0 O A:PRO42 4.9 30.0 1.0 N A:GLU43 4.9 32.4 1.0 NE A:ARG35 4.9 16.4 1.0 N A:PRO42 4.9 26.8 1.0

M.S.Chimenti, V.S.Khangulov, A.C.Robinson, J.L.Schlessman, E.B.Garcia-Moreno. Structural Consequences of the Ionization of Lysine Residues at 25 Internal Positions in A Protein. To Be Published.