Calcium in PDB 4wd1: Acetoacetyl-Coa Synthetase From Streptomyces Lividans

The structure of Acetoacetyl-Coa Synthetase From Streptomyces Lividans, PDB code: 4wd1 was solved by A.M.Gulick, C.A.Mitchell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.18 / 1.90
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	104.408, 104.408, 133.906, 90.00, 90.00, 120.00
R / Rfree (%)	16.1 / 19.4

The binding sites of Calcium atom in the Acetoacetyl-Coa Synthetase From Streptomyces Lividans (pdb code 4wd1). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Acetoacetyl-Coa Synthetase From Streptomyces Lividans, PDB code: 4wd1:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Acetoacetyl-Coa Synthetase From Streptomyces Lividans


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Acetoacetyl-Coa Synthetase From Streptomyces Lividans within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca723 b:36.5 occ:1.00 OG1 A:THR79 2.7 25.7 1.0 O A:THR79 2.7 22.0 1.0 OD2 A:ASP77 2.8 32.6 1.0 O2 A:EDO716 2.9 35.4 1.0 O A:PRO81 2.9 25.5 1.0 O A:HOH1294 3.0 45.0 1.0 C A:THR79 3.4 25.7 1.0 C2 A:EDO716 3.4 25.0 1.0 O A:GLY82 3.5 22.5 1.0 CG A:ASP77 3.6 30.1 1.0 C A:GLY82 3.7 24.8 1.0 CB A:THR79 3.8 33.0 1.0 OD1 A:ASP77 3.9 29.3 1.0 C A:PRO81 4.0 23.4 1.0 CA A:THR79 4.0 23.7 1.0 CA A:GLY82 4.1 20.8 1.0 C1 A:EDO716 4.2 37.3 1.0 N A:ALA83 4.2 15.5 1.0 N A:THR79 4.3 23.0 1.0 N A:MET80 4.3 18.6 1.0 N A:GLY82 4.5 21.6 1.0 CA A:MET80 4.6 19.0 1.0 CA A:ALA83 4.6 13.9 1.0 C A:MET80 4.8 22.5 1.0 CB A:ASP77 4.8 28.5 1.0

Calcium binding site 2 out of 2 in the Acetoacetyl-Coa Synthetase From Streptomyces Lividans


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Acetoacetyl-Coa Synthetase From Streptomyces Lividans within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca724 b:36.8 occ:1.00 O A:ILE550 2.6 33.5 1.0 O A:GLU545 2.8 37.1 1.0 O A:LEU547 2.8 38.2 1.0 O A:HOH1288 2.9 40.5 1.0 O A:HOH900 2.9 45.1 1.0 O A:HOH1287 3.0 40.4 1.0 C A:ILE550 3.7 38.4 1.0 C A:GLU545 3.8 37.8 1.0 C A:LEU547 3.8 44.8 1.0 O A:PRO548 4.1 34.6 1.0 CA A:PRO548 4.3 39.7 1.0 C A:PRO548 4.3 34.3 1.0 C A:ARG546 4.4 40.9 1.0 N A:PRO548 4.5 42.7 1.0 O A:ARG546 4.5 38.9 1.0 N A:ILE550 4.5 39.4 1.0 N A:LEU547 4.5 41.2 1.0 CA A:GLU545 4.5 35.1 1.0 N A:ARG551 4.6 37.8 1.0 CA A:ILE550 4.6 37.6 1.0 CA A:ARG551 4.6 31.6 1.0 O A:ARG551 4.7 35.6 1.0 N A:ARG546 4.7 35.7 1.0 CA A:ARG546 4.8 40.2 1.0 CA A:LEU547 4.8 40.7 1.0 C A:ARG551 4.9 38.4 1.0 CB A:ILE550 5.0 43.4 1.0

C.A.Mitchell, A.C.Tucker, J.C.Escalante-Semerena, A.M.Gulick. The Structure of S. Lividans Acetoacetyl-Coa Synthetase Shows A Novel Interaction Between the C-Terminal Extension and the N-Terminal Domain. Proteins 2014.
ISSN: ESSN 1097-0134
PubMed: 25488501
DOI: 10.1002/PROT.24738