Calcium in PDB 4awn: Structure of Recombinant Human Dnase I (Rhdnasei) in Complex with Magnesium and Phosphate.

All present enzymatic activity of Structure of Recombinant Human Dnase I (Rhdnasei) in Complex with Magnesium and Phosphate.:
3.1.21.1;

The structure of Structure of Recombinant Human Dnase I (Rhdnasei) in Complex with Magnesium and Phosphate., PDB code: 4awn was solved by G.Parsiegla, C.Noguere, L.Santell, R.A.Lazarus, Y.Bourne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.13 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.960, 58.660, 96.430, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 21.9

The structure of Structure of Recombinant Human Dnase I (Rhdnasei) in Complex with Magnesium and Phosphate. also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Calcium atom in the Structure of Recombinant Human Dnase I (Rhdnasei) in Complex with Magnesium and Phosphate. (pdb code 4awn). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Recombinant Human Dnase I (Rhdnasei) in Complex with Magnesium and Phosphate., PDB code: 4awn:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of Recombinant Human Dnase I (Rhdnasei) in Complex with Magnesium and Phosphate.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Recombinant Human Dnase I (Rhdnasei) in Complex with Magnesium and Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca300 b:34.8 occ:1.00 O A:HOH2101 2.1 21.8 1.0 O A:PHE109 2.1 19.7 1.0 OD2 A:ASP99 2.2 20.6 1.0 OD2 A:ASP107 2.2 30.2 1.0 OE1 A:GLU112 2.3 23.4 1.0 O A:HOH2100 2.3 31.5 1.0 CG A:ASP99 3.1 21.6 1.0 CG A:ASP107 3.2 32.3 1.0 OD1 A:ASP99 3.3 21.1 1.0 C A:PHE109 3.3 19.8 1.0 CD A:GLU112 3.4 26.4 1.0 CB A:ASP107 3.7 31.6 1.0 OE2 A:GLU112 3.9 28.8 1.0 N A:PHE109 3.9 21.7 1.0 OE2 A:GLU102 3.9 47.9 1.0 O A:ASN110 4.0 17.4 1.0 CA A:PHE109 4.1 20.2 1.0 OD1 A:ASP107 4.2 34.4 1.0 NE A:ARG73 4.3 26.7 1.0 C A:ASN110 4.3 18.4 1.0 N A:ASN110 4.3 19.0 1.0 CB A:PHE109 4.4 19.4 1.0 CA A:ASN110 4.5 19.4 1.0 CB A:ASP99 4.5 22.1 1.0 CG A:GLU112 4.5 20.0 1.0 CB A:GLU112 4.6 17.9 1.0 O A:HOH2065 4.6 25.0 1.0 N A:GLU112 4.7 16.5 1.0 CD A:GLU102 4.7 48.2 1.0 NH2 A:ARG73 4.7 26.6 1.0 CG A:GLU102 4.7 44.7 1.0 C A:ASP107 4.8 30.1 1.0 CA A:ASP107 4.9 31.6 1.0 N A:THR108 4.9 27.8 1.0 CZ A:ARG73 4.9 29.3 1.0 CG A:ARG73 4.9 31.3 1.0 O A:HOH2099 4.9 36.2 1.0

Calcium binding site 2 out of 2 in the Structure of Recombinant Human Dnase I (Rhdnasei) in Complex with Magnesium and Phosphate.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Recombinant Human Dnase I (Rhdnasei) in Complex with Magnesium and Phosphate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:20.5 occ:1.00 O A:THR207 2.3 21.6 1.0 O A:THR205 2.3 23.4 1.0 OD2 A:ASP201 2.4 21.8 1.0 O A:THR203 2.4 17.3 1.0 O A:HOH2169 2.5 17.5 1.0 O A:HOH2170 2.5 19.0 1.0 OD1 A:ASP201 2.6 18.2 1.0 OG1 A:THR203 2.7 18.2 1.0 CG A:ASP201 2.9 19.8 1.0 C A:THR203 3.4 17.9 1.0 C A:THR207 3.6 21.0 1.0 C A:THR205 3.6 23.3 1.0 CB A:THR203 3.8 17.5 1.0 CA A:THR203 4.0 17.6 1.0 N A:THR207 4.1 21.2 1.0 C A:PRO206 4.1 22.3 1.0 N A:THR203 4.2 16.8 1.0 N A:THR205 4.2 21.9 1.0 CA A:PRO206 4.4 22.8 1.0 N A:ALA204 4.4 18.6 1.0 CB A:ASP201 4.4 18.3 1.0 CA A:THR207 4.4 21.1 1.0 N A:PRO206 4.5 23.7 1.0 N A:HIS208 4.5 21.4 1.0 C A:ALA204 4.5 20.5 1.0 O A:PRO206 4.5 21.3 1.0 CA A:HIS208 4.5 21.9 1.0 O A:HOH2174 4.5 34.1 1.0 CA A:THR205 4.6 23.1 1.0 OG1 A:THR207 4.6 21.2 1.0 O A:HOH2171 4.7 36.7 1.0 CA A:ALA204 4.7 19.6 1.0 O A:HOH2172 4.8 27.2 1.0 CE2 A:TYR253 4.8 19.1 1.0 OH A:TYR253 4.8 20.4 1.0 OG1 A:THR205 4.9 24.5 1.0 CG2 A:THR203 4.9 16.6 1.0

G.Parsiegla, C.Noguere, L.Santell, R.A.Lazarus, Y.Bourne. The Structure of Human Dnase I Bound to Magnesium and Phosphate Ions Points to A Catalytic Mechanism Common to Members of the Dnase I-Like Superfamily. Biochemistry V. 51 10250 2012.
ISSN: ISSN 0006-2960
PubMed: 23215638
DOI: 10.1021/BI300873F