Calcium in PDB 5bv9: The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose

All present enzymatic activity of The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose:
3.2.1.91;

The structure of The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose, PDB code: 5bv9 was solved by P.M.Alahuhta, V.V.Lunin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.93
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	97.291, 97.291, 218.108, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 20.7

The binding sites of Calcium atom in the The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose (pdb code 5bv9). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose, PDB code: 5bv9:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca801 b:18.0 occ:0.94 O A:HOH1187 2.3 8.6 0.7 OE1 A:GLN181 2.3 9.3 1.0 OD2 A:ASP405 2.3 11.0 1.0 O A:GLN181 2.4 10.0 1.0 OE2 A:GLU186 2.4 12.9 1.0 O A:HOH1501 2.6 9.6 0.7 OE1 A:GLU186 2.6 14.8 1.0 CD A:GLU186 2.9 12.9 1.0 CG A:ASP405 3.4 11.5 1.0 C A:GLN181 3.5 9.5 1.0 CD A:GLN181 3.5 10.0 1.0 CB A:ASP405 3.8 12.0 1.0 CB A:GLN181 3.9 9.2 1.0 CA A:GLN181 4.0 9.7 1.0 NH1 A:ARG597 4.1 13.6 1.0 O A:HOH1624 4.2 40.7 1.0 CG A:GLN181 4.2 9.6 1.0 O A:HOH1525 4.3 29.7 1.0 N A:SER183 4.3 10.1 1.0 CG A:GLU186 4.4 12.7 1.0 NE2 A:GLN181 4.5 9.7 1.0 OD1 A:ASP405 4.5 11.6 1.0 N A:GLU182 4.6 8.9 1.0 OE1 A:GLU602 4.6 18.8 1.0 CB A:SER183 4.7 10.2 1.0 OG A:SER183 4.8 11.4 1.0 CA A:GLU182 4.8 9.7 1.0 CD A:GLU602 4.9 19.0 1.0

Calcium binding site 2 out of 3 in the The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca802 b:35.8 occ:0.62 O A:HOH1487 2.2 12.8 0.5 O A:ILE83 2.4 11.3 1.0 O A:GLU79 2.4 14.8 1.0 O A:HOH1096 2.7 7.1 0.8 O A:VAL85 2.8 25.1 1.0 OE1 A:GLU92 3.0 18.3 1.0 O A:LYS80 3.3 14.4 1.0 C A:ILE83 3.5 11.1 1.0 C A:LYS80 3.6 14.4 1.0 C A:GLU79 3.6 13.9 1.0 O A:HOH1487 3.6 22.7 0.5 N A:VAL85 3.7 15.6 1.0 O A:HOH1630 3.7 46.1 0.9 C A:VAL85 3.7 23.6 1.0 CA A:LYS80 3.9 14.4 1.0 CD A:GLU92 4.1 17.2 1.0 OH A:TYR172 4.2 11.8 1.0 CA A:PRO84 4.2 12.2 1.0 N A:LYS80 4.2 14.8 1.0 N A:PRO84 4.3 11.1 1.0 OE2 A:GLU92 4.3 15.7 1.0 C A:PRO84 4.4 14.4 1.0 CA A:VAL85 4.4 19.7 1.0 N A:TYR81 4.4 14.5 1.0 N A:ILE83 4.5 11.2 1.0 CA A:ILE83 4.5 11.4 1.0 N A:ASN86 4.6 30.8 1.0 CA A:ASN86 4.7 40.9 1.0 CB A:ASN86 4.7 43.6 1.0 CB A:ILE83 4.8 11.3 1.0 CA A:GLU79 4.8 15.8 1.0

Calcium binding site 3 out of 3 in the The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of The Structure of Bacillus Pumilus GH48 in Complex with Cellobiose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca803 b:30.1 occ:0.40 O A:HOH1390 2.2 45.1 1.0 O A:HOH1552 2.3 26.5 0.9 O A:HOH1615 2.4 31.7 0.9 O A:HOH1773 2.5 24.9 0.4 OG1 A:THR248 2.5 20.9 1.0 OD1 A:ASN246 2.6 16.4 1.0 O A:HOH1773 2.9 33.5 0.6 CG A:ASN246 3.4 16.6 1.0 ND2 A:ASN246 3.4 16.2 1.0 CB A:THR248 3.5 22.4 1.0 O A:HOH1831 3.9 47.0 0.9 O A:HOH1837 4.0 26.1 0.5 N A:THR248 4.2 16.8 1.0 CA A:THR248 4.5 19.9 1.0 O A:HOH1512 4.5 41.6 1.0 CG2 A:THR248 4.5 22.1 1.0 O A:HOH1846 4.6 19.1 0.3 CB A:ASN246 4.8 18.9 1.0 O A:HOH1449 4.9 23.5 0.9

M.Chen, L.Bu, M.Alahuhta, R.Brunecky, Q.Xu, V.V.Lunin, J.W.Brady, M.F.Crowley, M.E.Himmel, Y.J.Bomble. Strategies to Reduce End-Product Inhibition in Family 48 Glycoside Hydrolases. Proteins V. 84 295 2016.
ISSN: ESSN 1097-0134
PubMed: 26572060
DOI: 10.1002/PROT.24965