Zinc in PDB 3ii1: Structural Characterization of Difunctional Glucanase- Xylanse CELM2

All present enzymatic activity of Structural Characterization of Difunctional Glucanase- Xylanse CELM2:
3.2.1.4;

The structure of Structural Characterization of Difunctional Glucanase- Xylanse CELM2, PDB code: 3ii1 was solved by K.Y.Hwang, K.H.Nam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.64 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.594, 87.431, 110.574, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 22.1

The binding sites of Zinc atom in the Structural Characterization of Difunctional Glucanase- Xylanse CELM2 (pdb code 3ii1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Structural Characterization of Difunctional Glucanase- Xylanse CELM2, PDB code: 3ii1:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Structural Characterization of Difunctional Glucanase- Xylanse CELM2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Characterization of Difunctional Glucanase- Xylanse CELM2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn571 b:36.8 occ:1.00 OE2 A:GLU241 2.0 2.0 0.2 O A:HOH946 2.0 26.5 1.0 NE2 A:HIS233 2.0 22.6 1.0 O A:HOH947 2.2 36.3 1.0 CD A:GLU241 2.8 2.0 0.2 OE1 A:GLU241 3.0 2.0 0.2 CE1 A:HIS233 3.0 18.8 1.0 CD2 A:HIS233 3.0 22.7 1.0 O A:HOH948 3.0 33.5 1.0 CE A:LYS245 4.1 22.1 1.0 ND1 A:HIS233 4.1 21.7 1.0 CG A:HIS233 4.2 20.3 1.0 CG A:GLU241 4.2 3.4 0.2 CZ3 A:TRP225 4.2 12.6 1.0 O A:HOH949 4.3 37.8 1.0 NZ A:LYS245 4.3 13.8 1.0 O A:HOH755 4.5 22.9 1.0 CE3 A:TRP225 4.7 14.1 1.0 O A:ILE131 4.9 20.2 1.0

Zinc binding site 2 out of 3 in the Structural Characterization of Difunctional Glucanase- Xylanse CELM2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Characterization of Difunctional Glucanase- Xylanse CELM2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn572 b:29.6 occ:1.00 O A:HOH959 1.9 33.2 1.0 NE2 A:HIS286 2.0 24.0 1.0 O A:HOH960 2.1 18.9 1.0 CE1 A:HIS286 2.8 26.7 1.0 CD2 A:HIS286 3.1 25.9 1.0 O A:HOH961 3.6 42.0 1.0 ND1 A:HIS286 4.0 26.3 1.0 CG A:HIS286 4.1 24.3 1.0

Zinc binding site 3 out of 3 in the Structural Characterization of Difunctional Glucanase- Xylanse CELM2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structural Characterization of Difunctional Glucanase- Xylanse CELM2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn573 b:35.4 occ:1.00 OD1 A:ASP240 2.0 24.9 1.0 NE2 A:HIS297 2.1 24.1 1.0 O A:HOH921 2.5 23.7 1.0 OD2 A:ASP240 2.7 25.7 1.0 CG A:ASP240 2.7 21.6 1.0 CE1 A:HIS297 3.1 23.0 1.0 CD2 A:HIS297 3.1 20.1 1.0 O A:HOH729 3.9 48.1 1.0 CB A:ASP240 4.1 16.9 1.0 CZ2 A:TRP305 4.1 17.1 1.0 ND1 A:HIS297 4.2 23.9 1.0 CG A:HIS297 4.2 22.2 1.0 NH1 A:ARG243 4.4 18.1 1.0 CH2 A:TRP305 4.6 16.3 1.0 NH2 A:ARG243 4.7 20.8 1.0 ND2 A:ASN296 4.8 36.1 1.0 CA A:ASP240 4.9 17.3 1.0 CZ A:ARG243 4.9 20.4 1.0

K.H.Nam, W.H.Lee, K.H.Rhee, K.Y.Hwang. Structural Characterization of the Bifunctional Glucanase-Xylanase CELM2 Reveals the Metal Effect and Substrate-Binding Moiety Biochem.Biophys.Res.Commun. V. 391 1726 2010.
ISSN: ISSN 0006-291X
PubMed: 20043877
DOI: 10.1016/J.BBRC.2009.12.141