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Calcium in PDB 1ia7: Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose

Enzymatic activity of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose

All present enzymatic activity of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose:
3.2.1.4;

Protein crystallography data

The structure of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose, PDB code: 1ia7 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) 16.23 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.850, 52.380, 71.970, 90.00, 108.46, 90.00
R / Rfree (%) 16.8 / 22

Other elements in 1ia7:

The structure of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose also contains other interesting chemical elements:

Nickel (Ni) 1 atom
Zinc (Zn) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose (pdb code 1ia7). 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 the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose, PDB code: 1ia7:

Calcium binding site 1 out of 1 in 1ia7

Go back to Calcium Binding Sites List in 1ia7
Calcium binding site 1 out of 1 in the Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose


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 the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1332

b:8.0
occ:1.00
 O A:ASP257 2.3 8.0 1.0
O A:HOH1548 2.3 5.8 1.0
O A:HOH1638 2.3 5.6 1.0
OD2 A:ASP211 2.4 9.3 1.0
O A:SER208 2.5 9.9 1.0
OD2 A:ASP212 2.5 7.2 1.0
OG A:SER208 2.6 6.2 1.0
OD1 A:ASP211 2.9 5.9 1.0
CG A:ASP211 3.0 6.0 1.0
C A:ASP257 3.3 7.9 1.0
C A:SER208 3.3 10.0 1.0
CG A:ASP212 3.5 8.9 1.0
CB A:SER208 3.7 9.0 1.0
OD1 A:ASP212 3.8 7.2 1.0
CA A:SER208 3.9 10.4 1.0
CA A:ASP257 4.0 9.3 1.0
OD1 A:ASP257 4.1 7.1 1.0
N A:ASP258 4.1 7.4 1.0
N A:PHE209 4.1 9.7 1.0
N A:SER208 4.2 11.5 1.0
CA A:ASP258 4.3 6.7 1.0
CA A:PHE209 4.4 11.1 1.0
CB A:ASP153 4.5 6.3 1.0
CB A:ASP211 4.5 8.5 1.0
O A:HOH1392 4.6 12.3 1.0
N A:MET259 4.6 7.9 1.0
CG A:ASP257 4.6 10.7 1.0
O A:TRP256 4.7 7.9 1.0
CB A:ASP212 4.8 5.8 1.0
N A:ASP212 4.8 6.8 1.0
CB A:ASP257 5.0 9.5 1.0
C A:ASP258 5.0 7.3 1.0

Reference:

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
Page generated: Mon Jul 7 15:48:52 2025

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