Nickel in PDB 1ia6: Crystal Structure of the Cellulase CEL9M of C. Cellulolyticum

All present enzymatic activity of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticum:
3.2.1.4;

The structure of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticum, PDB code: 1ia6 was solved by G.Parsiegla, A.Belaich, J.P.Belaich, R.Haser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.24 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.350, 53.010, 71.680, 90.00, 108.70, 90.00
R / Rfree (%)	15.8 / 18.9

The structure of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticum also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Zinc	(Zn)	1 atom

The binding sites of Nickel atom in the Crystal Structure of the Cellulase CEL9M of C. Cellulolyticum (pdb code 1ia6). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of the Cellulase CEL9M of C. Cellulolyticum, PDB code: 1ia6:

Nickel binding site 1 out of 1 in the Crystal Structure of the Cellulase CEL9M of C. Cellulolyticum


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticum within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni1265 b:24.7 occ:1.00 OD2 A:ASP343 2.0 22.2 1.0 O A:HOH1497 2.1 35.9 1.0 NE2 A:HIS4 2.1 23.0 1.0 N A:ALA1 2.2 26.7 1.0 O A:ALA1 2.4 24.9 1.0 CG A:ASP343 2.8 19.8 1.0 CA A:ALA1 2.9 26.8 1.0 C A:ALA1 3.0 26.2 1.0 CE1 A:HIS4 3.1 24.0 1.0 CD2 A:HIS4 3.1 23.8 1.0 OD1 A:ASP343 3.1 19.9 1.0 CB A:ALA1 3.4 26.1 1.0 O A:HOH1431 4.1 31.7 1.0 ND1 A:HIS4 4.2 23.5 1.0 OD2 A:ASP338 4.2 14.2 1.0 CG A:HIS4 4.2 23.5 1.0 CB A:ASP343 4.2 15.4 1.0 N A:GLY2 4.3 26.5 1.0 CB A:ASP338 4.4 12.4 1.0 CG A:ASP338 4.4 14.6 1.0

G.Parsiegla, A.Belaich, J.P.Belaich, R.Haser. Crystal Structure of the Cellulase CEL9M Enlightens Structure/Function Relationships of the Variable Catalytic Modules in Glycoside Hydrolases. Biochemistry V. 41 11134 2002.
ISSN: ISSN 0006-2960
PubMed: 12220178
DOI: 10.1021/BI025816M