Calcium in PDB 6ms2: Crystal Structure of the GH43 Blxynb Protein From Bacillus Licheniformis

The structure of Crystal Structure of the GH43 Blxynb Protein From Bacillus Licheniformis, PDB code: 6ms2 was solved by L.M.Zanphorlin, M.A.B.Morais, J.A.Diogo, M.T.Murakami, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.31 / 2.49
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	152.858, 41.902, 71.805, 90.00, 91.70, 90.00
R / Rfree (%)	19.7 / 24.2

The binding sites of Calcium atom in the Crystal Structure of the GH43 Blxynb Protein From Bacillus Licheniformis (pdb code 6ms2). 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 the GH43 Blxynb Protein From Bacillus Licheniformis, PDB code: 6ms2:

Calcium binding site 1 out of 1 in the Crystal Structure of the GH43 Blxynb Protein From Bacillus Licheniformis


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 the GH43 Blxynb Protein From Bacillus Licheniformis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca601 b:73.6 occ:1.00 OD1 A:ASP319 2.4 39.1 1.0 O A:GLY347 2.4 40.9 1.0 O A:ASP319 2.4 32.2 1.0 OD2 A:ASP508 2.5 40.4 1.0 O A:ASP508 3.1 40.1 1.0 CG A:ASP319 3.2 39.8 1.0 C A:GLY347 3.3 38.5 1.0 CA A:GLY347 3.5 38.3 1.0 C A:ASP319 3.6 32.1 1.0 CG A:ASP508 3.6 39.5 1.0 CB A:ASP319 4.0 36.8 1.0 OD2 A:ASP319 4.0 43.3 1.0 C A:ASP508 4.1 37.8 1.0 CA A:ASP319 4.1 33.5 1.0 OD1 A:ASP508 4.2 40.8 1.0 CA A:ASP508 4.5 37.0 1.0 N A:TYR348 4.6 37.8 1.0 CB A:ASP508 4.6 37.1 1.0 N A:PHE320 4.7 32.1 1.0 C A:PHE320 4.7 38.4 1.0 O A:PHE320 4.9 41.2 1.0 N A:ASP321 4.9 40.9 1.0 N A:GLY347 5.0 40.0 1.0

L.M.Zanphorlin, M.A.B.De Morais, J.A.Diogo, M.N.Domingues, F.H.M.De Souza, R.Ruller, M.T.Murakami. Structure-Guided Design Combined with Evolutionary Diversity Led to the Discovery of the Xylose-Releasing Exo-Xylanase Activity in the Glycoside Hydrolase Family 43. Biotechnol. Bioeng. V. 116 734 2019.
ISSN: ESSN 1097-0290
PubMed: 30556897
DOI: 10.1002/BIT.26899