Calcium in PDB 6hos: Structure of the KPFLO2 Adhesin Domain in Complex with Glycerol

The structure of Structure of the KPFLO2 Adhesin Domain in Complex with Glycerol, PDB code: 6hos was solved by L.-O.Essen, M.Kock, M.Veelders, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.41 / 2.15
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	79.943, 103.186, 72.099, 90.00, 113.51, 90.00
R / Rfree (%)	17.2 / 19.9

The structure of Structure of the KPFLO2 Adhesin Domain in Complex with Glycerol also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Calcium atom in the Structure of the KPFLO2 Adhesin Domain in Complex with Glycerol (pdb code 6hos). 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 the KPFLO2 Adhesin Domain in Complex with Glycerol, PDB code: 6hos:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of the KPFLO2 Adhesin Domain in Complex with Glycerol


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the KPFLO2 Adhesin Domain in Complex with Glycerol within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:40.8 occ:0.91 O A:GLU216 2.3 33.5 1.0 OD1 A:ASN214 2.4 26.9 1.0 OD1 A:ASP146 2.4 33.9 1.0 O A:HIS218 2.4 39.6 1.0 OD2 A:ASP147 2.5 56.9 1.0 O2 A:GOL302 2.6 74.9 1.0 CG A:ASP146 3.2 34.8 1.0 C3 A:GOL302 3.3 79.9 1.0 O3 A:GOL302 3.3 81.1 1.0 C A:GLU216 3.5 39.6 1.0 C2 A:GOL302 3.5 78.1 1.0 CG A:ASP147 3.5 50.7 1.0 CG A:ASN214 3.5 33.2 1.0 C A:HIS218 3.5 40.6 1.0 OD2 A:ASP146 3.6 39.3 1.0 N A:GLU216 3.8 29.6 1.0 N A:HIS218 3.9 35.5 1.0 C A:ARG217 4.0 38.3 1.0 ND2 A:ASN214 4.1 30.7 1.0 O A:ARG217 4.1 37.0 1.0 OD1 A:ASP147 4.1 58.0 1.0 CA A:HIS218 4.2 38.4 1.0 CA A:GLU216 4.3 37.8 1.0 N A:ASP147 4.3 24.2 1.0 C A:ASP146 4.3 29.8 1.0 N A:ILE215 4.3 31.6 1.0 CB A:ASP147 4.4 32.6 1.0 N A:ARG217 4.4 39.9 1.0 O A:ASP146 4.5 29.7 1.0 CB A:ASP146 4.5 29.9 1.0 N A:ALA219 4.6 37.3 1.0 CA A:ASP147 4.6 26.0 1.0 CA A:ARG217 4.7 42.0 1.0 C1 A:GOL302 4.7 81.2 1.0 CB A:ASN214 4.7 29.4 1.0 CB A:HIS218 4.8 36.8 1.0 CG A:GLU216 4.8 58.0 1.0 CA A:ASN214 4.9 23.8 1.0 CA A:ASP146 4.9 28.8 1.0 CA A:ALA219 4.9 35.6 1.0 C A:ILE215 4.9 34.8 1.0 CB A:ARG217 4.9 44.8 1.0 O1 A:GOL302 5.0 84.9 1.0

Calcium binding site 2 out of 2 in the Structure of the KPFLO2 Adhesin Domain in Complex with Glycerol


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of the KPFLO2 Adhesin Domain in Complex with Glycerol within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca301 b:36.4 occ:0.73 O B:GLU216 2.3 33.3 1.0 O B:HIS218 2.3 36.0 1.0 OD1 B:ASN214 2.4 28.5 1.0 OD1 B:ASP146 2.4 31.4 1.0 O1 B:GOL302 2.5 48.8 0.9 OD1 B:ASP147 2.5 58.2 1.0 O2 B:GOL302 3.0 62.1 0.9 CG B:ASP146 3.2 34.8 1.0 C1 B:GOL302 3.4 55.3 0.9 CG B:ASN214 3.5 30.9 1.0 C B:HIS218 3.5 39.1 1.0 C B:GLU216 3.5 40.6 1.0 CG B:ASP147 3.5 55.1 1.0 OD2 B:ASP146 3.5 36.0 1.0 C2 B:GOL302 3.6 62.6 0.9 N B:HIS218 3.9 36.4 1.0 N B:GLU216 3.9 39.0 1.0 C B:ARG217 3.9 38.7 1.0 OE2 B:GLU216 4.0 88.4 1.0 ND2 B:ASN214 4.0 29.9 1.0 O B:ARG217 4.0 36.3 1.0 OD2 B:ASP147 4.1 60.4 1.0 CA B:HIS218 4.2 38.8 1.0 N B:ASP147 4.3 26.8 1.0 C B:ASP146 4.3 30.4 1.0 CA B:GLU216 4.4 41.4 1.0 CD B:GLU216 4.4 80.8 1.0 N B:ILE215 4.4 30.1 1.0 N B:ARG217 4.4 36.0 1.0 CB B:ASP146 4.4 26.7 1.0 CB B:ASP147 4.4 36.5 1.0 O B:ASP146 4.5 29.2 1.0 N B:ALA219 4.5 37.8 1.0 CA B:ARG217 4.6 41.9 1.0 CA B:ASP147 4.7 28.5 1.0 OE1 B:GLU216 4.7 90.5 1.0 CB B:ASN214 4.7 25.7 1.0 CB B:HIS218 4.8 36.2 1.0 CA B:ALA219 4.8 36.9 1.0 CA B:ASP146 4.8 26.0 1.0 CA B:ASN214 4.9 24.6 1.0 CB B:ARG217 5.0 47.0 1.0

M.Kock, S.Bruckner, N.Wozniak, M.Maestre-Reyna, M.Veelders, J.Schlereth, H.U.Mosch, L.O.Essen. Structural and Functional Characterization of PA14/FLO5-Like Adhesins Fromkomagataella Pastoris. Front Microbiol V. 9 2581 2018.
ISSN: ESSN 1664-302X
PubMed: 30425696
DOI: 10.3389/FMICB.2018.02581