Calcium in PDB 4mz0: Structure of A Ketosynthase-Acyltransferase Di-Domain From Module Curl of the Curacin A Polyketide Synthase

All present enzymatic activity of Structure of A Ketosynthase-Acyltransferase Di-Domain From Module Curl of the Curacin A Polyketide Synthase:
2.3.1.41;

The structure of Structure of A Ketosynthase-Acyltransferase Di-Domain From Module Curl of the Curacin A Polyketide Synthase, PDB code: 4mz0 was solved by J.R.Whicher, S.S.Smaga, J.L.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.99 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.265, 150.704, 236.005, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 23.1

The binding sites of Calcium atom in the Structure of A Ketosynthase-Acyltransferase Di-Domain From Module Curl of the Curacin A Polyketide Synthase (pdb code 4mz0). 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 A Ketosynthase-Acyltransferase Di-Domain From Module Curl of the Curacin A Polyketide Synthase, PDB code: 4mz0:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of A Ketosynthase-Acyltransferase Di-Domain From Module Curl of the Curacin A Polyketide Synthase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of A Ketosynthase-Acyltransferase Di-Domain From Module Curl of the Curacin A Polyketide Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1001 b:42.7 occ:1.00 O A:VAL314 2.3 41.3 1.0 O A:GLY311 2.4 45.3 1.0 O A:HOH1222 2.5 31.2 1.0 OD2 A:ASP306 2.5 57.4 1.0 O A:HOH1265 2.5 27.3 1.0 O A:HOH1266 2.6 49.1 1.0 O A:LEU312 3.3 47.8 1.0 CG A:ASP306 3.4 48.5 1.0 C A:VAL314 3.4 42.0 1.0 CB A:ASP306 3.6 34.0 1.0 C A:GLY311 3.6 45.2 1.0 C A:LEU312 3.7 46.0 1.0 N A:VAL314 3.8 40.7 1.0 CA A:LEU312 4.1 39.2 1.0 CA A:VAL314 4.2 39.2 1.0 CA A:GLY453 4.2 30.1 1.0 N A:THR313 4.3 41.9 1.0 N A:LEU312 4.3 39.5 1.0 N A:PRO315 4.4 37.6 1.0 OD1 A:ASP306 4.5 52.0 1.0 C A:THR313 4.5 46.7 1.0 CA A:PRO315 4.6 37.2 1.0 O A:HOH1110 4.6 31.3 1.0 N A:GLY453 4.6 30.8 1.0 O A:GLY310 4.7 46.5 1.0 C A:PRO315 4.7 44.1 1.0 CA A:THR313 4.8 41.6 1.0 CA A:GLY311 4.8 42.4 1.0 O A:SER309 4.8 41.2 1.0 N A:GLY311 4.9 43.1 1.0 C A:GLY310 4.9 46.6 1.0 CB A:VAL314 4.9 41.7 1.0 O A:PRO315 4.9 45.2 1.0

Calcium binding site 2 out of 2 in the Structure of A Ketosynthase-Acyltransferase Di-Domain From Module Curl of the Curacin A Polyketide Synthase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of A Ketosynthase-Acyltransferase Di-Domain From Module Curl of the Curacin A Polyketide Synthase within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1001 b:53.2 occ:1.00 O B:HOH1215 2.2 56.8 1.0 OD2 B:ASP306 2.2 49.3 1.0 O B:VAL314 2.3 42.1 1.0 O B:HOH1177 2.4 32.2 1.0 O B:HOH1214 2.4 50.4 1.0 O B:GLY311 2.4 40.2 1.0 CG B:ASP306 3.3 42.7 1.0 C B:VAL314 3.5 42.1 1.0 O B:LEU312 3.5 42.6 1.0 C B:GLY311 3.6 42.2 1.0 CB B:ASP306 3.6 36.7 1.0 C B:LEU312 3.8 43.1 1.0 N B:VAL314 3.9 40.5 1.0 CA B:LEU312 4.2 36.5 1.0 CA B:VAL314 4.2 39.0 1.0 N B:LEU312 4.3 36.8 1.0 OD1 B:ASP306 4.4 42.2 1.0 N B:THR313 4.4 42.1 1.0 N B:GLY311 4.4 45.3 1.0 N B:PRO315 4.5 38.2 1.0 CA B:PRO315 4.5 38.0 1.0 O B:HOH1114 4.5 26.1 1.0 CA B:GLY453 4.6 35.0 1.0 C B:THR313 4.6 46.7 1.0 C B:GLY310 4.6 49.6 1.0 C B:PRO315 4.6 43.1 1.0 CA B:GLY311 4.7 43.5 1.0 N B:GLY453 4.8 35.9 1.0 O B:PRO315 4.8 42.9 1.0 CB B:VAL314 4.9 42.1 1.0 CA B:THR313 4.9 42.3 1.0 O B:HOH1165 4.9 39.6 1.0 O B:GLY310 5.0 48.0 1.0 CA B:GLY310 5.0 48.5 1.0

J.R.Whicher, S.S.Smaga, D.A.Hansen, W.C.Brown, W.H.Gerwick, D.H.Sherman, J.L.Smith. Cyanobacterial Polyketide Synthase Docking Domains: A Tool For Engineering Natural Product Biosynthesis. Chem.Biol. V. 20 1340 2013.
ISSN: ISSN 1074-5521
PubMed: 24183970
DOI: 10.1016/J.CHEMBIOL.2013.09.015