Magnesium in PDB 3voi: CCCEL6A Catalytic Domain Complexed with P-Nitrophenyl Beta-D- Cellotrioside

All present enzymatic activity of CCCEL6A Catalytic Domain Complexed with P-Nitrophenyl Beta-D- Cellotrioside:
3.2.1.91;

The structure of CCCEL6A Catalytic Domain Complexed with P-Nitrophenyl Beta-D- Cellotrioside, PDB code: 3voi was solved by M.Tamura, T.Miyazaki, Y.Tanaka, M.Yoshida, A.Nishikawa, T.Tonozuka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.72 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.973, 71.502, 101.121, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 25.2

The binding sites of Magnesium atom in the CCCEL6A Catalytic Domain Complexed with P-Nitrophenyl Beta-D- Cellotrioside (pdb code 3voi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the CCCEL6A Catalytic Domain Complexed with P-Nitrophenyl Beta-D- Cellotrioside, PDB code: 3voi:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the CCCEL6A Catalytic Domain Complexed with P-Nitrophenyl Beta-D- Cellotrioside


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of CCCEL6A Catalytic Domain Complexed with P-Nitrophenyl Beta-D- Cellotrioside within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:25.2 occ:1.00 O A:HOH770 2.1 15.5 1.0 O A:HOH772 2.1 13.0 1.0 O A:HOH769 2.2 15.9 1.0 O A:HOH731 2.2 28.3 1.0 O A:HOH771 2.2 18.5 1.0 O A:HOH699 2.3 16.8 1.0 OG A:SER170 3.8 22.5 1.0 O A:HOH682 3.9 19.0 1.0 O4A A:RCB503 4.1 14.7 1.0 OG A:SER293 4.2 17.6 1.0 CB A:SER293 4.4 14.2 1.0 OD1 A:ASP388 4.4 16.5 1.0 NZ A:LYS382 4.5 16.9 1.0 O A:ASP388 4.5 15.3 1.0 OH A:TYR158 4.5 15.9 1.0 CB A:SER170 4.7 21.3 1.0 CA A:ASP388 4.7 14.2 1.0 O A:HOH665 4.7 14.2 1.0 CB A:ASP388 4.9 14.0 1.0

Magnesium binding site 2 out of 2 in the CCCEL6A Catalytic Domain Complexed with P-Nitrophenyl Beta-D- Cellotrioside


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of CCCEL6A Catalytic Domain Complexed with P-Nitrophenyl Beta-D- Cellotrioside within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:24.1 occ:1.00 O A:GLY309 2.0 15.8 1.0 O A:HOH768 2.1 20.6 1.0 O A:HOH690 2.2 15.2 1.0 C A:GLY309 3.2 15.6 1.0 O A:HOH685 4.1 25.2 1.0 N A:ASN310 4.1 15.3 1.0 CA A:ASN310 4.2 15.3 1.0 CA A:GLY309 4.2 15.9 1.0 OD1 A:ASP311 4.2 20.1 1.0 N A:ASP311 4.3 16.1 1.0 ND2 A:ASN262 4.4 22.1 1.0 OD2 A:ASP311 4.4 19.8 1.0 CG A:ASP311 4.4 17.7 1.0 CZ3 A:TRP261 4.7 14.3 1.0 C A:ASN310 4.7 15.7 1.0 O A:HOH738 4.9 23.3 1.0 CE3 A:TRP261 4.9 13.6 1.0 O A:HOH828 4.9 32.5 1.0

M.Tamura, T.Miyazaki, Y.Tanaka, M.Yoshida, A.Nishikawa, T.Tonozuka. Comparison of the Structural Changes in Two Cellobiohydrolases, CCCEL6A and CCCEL6C, From Coprinopsis Cinerea - A Tweezer-Like Motion in the Structure of CCCEL6C Febs J. V. 279 1871 2012.
ISSN: ISSN 1742-464X
PubMed: 22429290
DOI: 10.1111/J.1742-4658.2012.08568.X