Calcium in PDB 5bvu: Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase

All present enzymatic activity of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase:
3.2.1.21;

The structure of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase, PDB code: 5bvu was solved by R.Charoenwattanasatien, S.Pengthaisong, S.Sansenya, R.Mutoh, H.Tanaka, G.Kurisu, J.R.Ketudat Cairns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.61
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	177.683, 54.271, 83.180, 90.00, 90.00, 90.00
R / Rfree (%)	15.4 / 17.5

The binding sites of Calcium atom in the Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase (pdb code 5bvu). 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 Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase, PDB code: 5bvu:

Calcium binding site 1 out of 1 in the Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase


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 Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1017 b:25.5 occ:1.00 OD1 A:ASP583 2.3 28.9 1.0 O A:ILE581 2.3 22.8 1.0 OD1 A:ASP575 2.3 28.2 1.0 OD1 A:ASP579 2.3 25.9 1.0 OD1 A:ASP577 2.4 35.7 1.0 O A:HOH1155 2.5 30.2 1.0 O3 A:GOL1012 3.0 48.2 1.0 CG A:ASP579 3.1 26.7 1.0 CG A:ASP583 3.2 30.0 1.0 CG A:ASP575 3.3 25.9 1.0 C A:ILE581 3.4 23.2 1.0 OD2 A:ASP579 3.5 28.1 1.0 OD2 A:ASP583 3.6 35.8 1.0 CG A:ASP577 3.6 38.2 1.0 CA A:ASP575 3.9 27.3 1.0 N A:ILE581 3.9 22.8 1.0 CB A:ASP575 4.0 26.7 1.0 CA A:ILE581 4.1 23.1 1.0 N A:ASP579 4.1 28.0 1.0 N A:LYS576 4.1 33.9 1.0 OD2 A:ASP577 4.1 39.6 1.0 N A:ASP577 4.2 37.1 1.0 OD2 A:ASP575 4.2 27.4 1.0 N A:ASP583 4.2 24.6 1.0 CB A:ILE581 4.2 24.0 1.0 C A:PRO582 4.3 24.6 1.0 CB A:ASP579 4.3 27.2 1.0 C A:ASP575 4.3 30.1 1.0 C3 A:GOL1012 4.3 48.0 1.0 CB A:ASP583 4.4 28.2 1.0 N A:PRO582 4.5 22.4 1.0 O A:PRO582 4.5 24.5 1.0 CA A:ASP583 4.5 26.0 1.0 OG1 A:THR600 4.6 22.9 1.0 N A:ASN578 4.6 35.5 1.0 CA A:ASP579 4.6 27.5 1.0 CA A:PRO582 4.6 22.8 1.0 CB A:ASP577 4.7 37.2 1.0 N A:GLY580 4.7 23.5 1.0 CA A:ASP577 4.8 37.0 1.0 C A:ASP579 4.8 26.1 1.0 C A:ASP577 4.8 36.6 1.0

R.Charoenwattanasatien, S.Pengthaisong, I.Breen, R.Mutoh, S.Sansenya, Y.Hua, A.Tankrathok, L.Wu, C.Songsiriritthigul, H.Tanaka, S.J.Williams, G.J.Davies, G.Kurisu, J.R.Ketudat Cairns. Bacterial Beta-Glucosidase Reveals the Structural and Functional Basis of Genetic Defects in Human Glucocerebrosidase 2 (GBA2). Acs Chem.Biol. V. 11 1891 2016.
ISSN: ESSN 1554-8937
PubMed: 27115290
DOI: 10.1021/ACSCHEMBIO.6B00192