Calcium in PDB 2w67: BTGH84 in Complex with FMA34

All present enzymatic activity of BTGH84 in Complex with FMA34:
3.2.1.52;

The structure of BTGH84 in Complex with FMA34, PDB code: 2w67 was solved by Y.He, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	87.71 / 2.25
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	51.248, 92.101, 98.292, 103.42, 95.11, 100.60
R / Rfree (%)	18.1 / 22.9

The binding sites of Calcium atom in the BTGH84 in Complex with FMA34 (pdb code 2w67). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the BTGH84 in Complex with FMA34, PDB code: 2w67:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the BTGH84 in Complex with FMA34


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of BTGH84 in Complex with FMA34 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1718 b:25.7 occ:1.00 O A:GLU32 2.4 27.8 1.0 OE1 A:GLU61 2.5 22.9 1.0 OD2 A:ASP64 2.7 18.0 1.0 OD1 A:ASP64 2.7 20.6 1.0 CG A:ASP64 3.0 21.0 1.0 C A:GLU32 3.6 28.4 1.0 CD A:GLU61 3.6 21.9 1.0 CB A:GLU61 4.0 21.6 1.0 CA A:ALA33 4.0 25.2 1.0 CG A:GLU61 4.1 21.6 1.0 N A:ALA33 4.2 26.5 1.0 O A:HOH2011 4.3 24.9 1.0 N A:GLU61 4.4 20.5 1.0 C A:ALA33 4.4 24.3 1.0 CB A:ASP64 4.5 21.9 1.0 N A:ASN34 4.6 23.1 1.0 OE2 A:GLU61 4.6 18.8 1.0 CA A:GLU32 4.7 30.1 1.0 CA A:GLU61 4.8 21.8 1.0 CG A:GLU32 4.8 33.5 1.0 CG A:GLU97 4.9 24.6 1.0 CB A:GLU32 5.0 30.8 1.0

Calcium binding site 2 out of 2 in the BTGH84 in Complex with FMA34


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of BTGH84 in Complex with FMA34 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1590 b:32.7 occ:1.00 O B:GLU32 2.3 27.9 1.0 OE1 B:GLU61 2.4 29.7 1.0 OD2 B:ASP64 2.4 21.2 1.0 OD1 B:ASP64 2.5 25.2 1.0 CG B:ASP64 2.8 26.0 1.0 C B:GLU32 3.5 29.2 1.0 CD B:GLU61 3.6 31.5 1.0 CB B:GLU61 4.1 29.6 1.0 CA B:ALA33 4.2 26.4 1.0 CG B:GLU61 4.3 30.3 1.0 N B:ALA33 4.3 28.0 1.0 CB B:ASP64 4.3 27.1 1.0 N B:GLU61 4.4 28.4 1.0 OE2 B:GLU61 4.5 30.3 1.0 CA B:GLU32 4.6 31.2 1.0 C B:ALA33 4.7 25.6 1.0 CB B:GLU32 4.7 31.8 1.0 OE2 B:GLU97 4.8 31.3 1.0 CA B:GLU61 4.8 29.5 1.0 CG B:GLU32 4.9 35.3 1.0 N B:ASN34 4.9 24.7 1.0

F.Marcelo, Y.He, S.A.Yuzwa, L.Nieto, J.Jimenez-Barbero, M.Sollogoub, D.J.Vocadlo, G.J.Davies, Y.Bleriot. Molecular Basis For Inhibition of GH84 Glycoside Hydrolases By Substituted Azepanes: Conformational Flexibility Enables Probing of Substrate Distortion. J.Am.Chem.Soc. V. 131 5390 2009.
ISSN: ISSN 0002-7863
PubMed: 19331390
DOI: 10.1021/JA809776R