Calcium in PDB 1k72: The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose

All present enzymatic activity of The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose:
3.2.1.4;

The structure of The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose, PDB code: 1k72 was solved by D.Mandelman, A.Belaich, J.P.Belaich, N.Aghajari, H.Driguez, R.Haser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.31 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	57.000, 57.600, 86.800, 93.60, 100.80, 99.50
R / Rfree (%)	16.6 / 19.8

The structure of The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Calcium atom in the The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose (pdb code 1k72). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose, PDB code: 1k72:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca778 b:15.9 occ:1.00 OE1 A:GLU503 2.3 15.8 1.0 OD1 A:ASN581 2.3 14.8 1.0 O A:ASN578 2.3 15.6 1.0 O A:ASP500 2.4 13.4 1.0 OD1 A:ASP582 2.5 15.6 1.0 O A:HOH803 2.5 13.3 1.0 OE2 A:GLU503 3.0 12.4 1.0 CD A:GLU503 3.0 14.4 1.0 C A:ASN578 3.4 17.0 1.0 CG A:ASP582 3.4 11.9 1.0 CG A:ASN581 3.4 14.2 1.0 C A:ASP500 3.6 14.3 1.0 OD2 A:ASP582 3.7 13.2 1.0 ND2 A:ASN581 3.9 13.2 1.0 CA A:ASN578 4.2 17.1 1.0 N A:ASP500 4.2 13.3 1.0 N A:ASN578 4.3 15.3 1.0 CA A:ASP500 4.3 13.3 1.0 N A:PRO579 4.3 16.7 1.0 CB A:ASN578 4.4 15.8 1.0 CA A:PRO579 4.4 16.3 1.0 N A:ASP582 4.4 13.9 1.0 CB A:ASP500 4.4 14.5 1.0 CG A:GLU503 4.5 13.5 1.0 CD2 A:LEU501 4.5 11.8 1.0 N A:LEU501 4.5 11.3 1.0 C A:ASN581 4.6 14.2 1.0 CA A:LEU501 4.6 13.7 1.0 CB A:ASP582 4.7 12.4 1.0 N A:ASN581 4.7 14.6 1.0 CB A:ASN581 4.7 14.6 1.0 C A:PRO579 4.8 17.8 1.0 CA A:ASP582 4.8 13.2 1.0 CG A:ASN578 4.9 14.9 1.0 CA A:ASN581 4.9 16.0 1.0

Calcium binding site 2 out of 4 in the The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca779 b:12.1 occ:1.00 OD2 A:ASP213 2.3 10.4 1.0 O A:HOH1140 2.4 12.3 1.0 OD2 A:ASP212 2.4 11.7 1.0 O A:ASP259 2.5 10.8 1.0 O A:HOH785 2.5 12.0 1.0 O A:SER209 2.5 10.7 1.0 OG A:SER209 2.5 9.2 1.0 OD1 A:ASP212 2.6 10.5 1.0 CG A:ASP212 2.9 11.5 1.0 C A:SER209 3.3 12.7 1.0 CG A:ASP213 3.4 13.2 1.0 C A:ASP259 3.4 11.1 1.0 CB A:SER209 3.7 11.8 1.0 OD1 A:ASP213 3.7 11.9 1.0 CA A:SER209 3.9 11.0 1.0 N A:ASP260 4.1 11.3 1.0 N A:PHE210 4.2 11.0 1.0 CA A:ASP259 4.2 11.9 1.0 N A:SER209 4.2 11.4 1.0 OD2 A:ASP259 4.3 10.0 1.0 CA A:ASP260 4.3 13.5 1.0 CA A:PHE210 4.4 12.6 1.0 CB A:ASP212 4.4 11.9 1.0 N A:ASP213 4.5 11.1 1.0 CB A:ASP213 4.6 10.3 1.0 OG A:SER207 4.6 9.1 1.0 CB A:ALA151 4.7 9.4 1.0 N A:VAL261 4.8 11.9 1.0 O A:TRP258 4.8 10.9 1.0 O A:HOH857 4.9 14.8 1.0 CG A:ASP259 4.9 10.0 1.0

Calcium binding site 3 out of 4 in the The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca615 b:15.3 occ:1.00 O B:ASN578 2.2 14.2 1.0 OD1 B:ASN581 2.3 14.4 1.0 OE2 B:GLU503 2.3 11.7 1.0 O B:ASP500 2.4 14.6 1.0 OD1 B:ASP582 2.4 11.4 1.0 O B:HOH701 2.4 15.7 1.0 CD B:GLU503 3.0 12.2 1.0 OE1 B:GLU503 3.0 10.7 1.0 C B:ASN578 3.3 12.5 1.0 CG B:ASN581 3.4 13.4 1.0 CG B:ASP582 3.4 12.1 1.0 C B:ASP500 3.6 13.9 1.0 OD2 B:ASP582 3.7 11.0 1.0 ND2 B:ASN581 3.8 13.1 1.0 CA B:ASN578 4.2 11.4 1.0 N B:ASN578 4.2 12.2 1.0 CB B:ASN578 4.3 11.4 1.0 N B:ASP500 4.3 14.0 1.0 N B:PRO579 4.3 14.3 1.0 CA B:ASP500 4.3 14.8 1.0 CA B:PRO579 4.4 13.2 1.0 CB B:ASP500 4.4 15.9 1.0 N B:ASP582 4.5 13.7 1.0 CG B:GLU503 4.5 12.5 1.0 N B:LEU501 4.6 14.1 1.0 CD2 B:LEU501 4.6 10.6 1.0 CA B:LEU501 4.6 12.5 1.0 C B:ASN581 4.6 13.8 1.0 N B:ASN581 4.7 13.4 1.0 CB B:ASN581 4.7 14.2 1.0 CB B:ASP582 4.7 11.9 1.0 C B:PRO579 4.8 14.8 1.0 CG B:ASN578 4.9 12.6 1.0 CA B:ASP582 4.9 12.7 1.0 CA B:ASN581 4.9 14.0 1.0

Calcium binding site 4 out of 4 in the The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of The X-Ray Crystal Structure of CEL9G Complexed with Cellotriose within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca616 b:16.2 occ:1.00 OD1 B:ASP213 2.4 15.2 1.0 OD2 B:ASP212 2.4 14.2 1.0 O B:ASP259 2.4 11.4 1.0 O B:HOH976 2.4 12.8 1.0 O B:SER209 2.5 12.1 1.0 O B:HOH657 2.5 12.0 1.0 OG B:SER209 2.5 14.1 1.0 OD1 B:ASP212 2.6 13.2 1.0 CG B:ASP212 2.9 14.6 1.0 C B:SER209 3.3 15.0 1.0 C B:ASP259 3.4 12.9 1.0 CG B:ASP213 3.4 13.2 1.0 CB B:SER209 3.6 16.2 1.0 OD2 B:ASP213 3.8 14.1 1.0 CA B:SER209 3.9 15.3 1.0 N B:ASP260 4.1 10.6 1.0 N B:SER209 4.2 15.3 1.0 N B:PHE210 4.2 12.9 1.0 CA B:ASP259 4.2 12.0 1.0 CA B:ASP260 4.3 12.0 1.0 OD1 B:ASP259 4.3 13.1 1.0 CB B:ASP212 4.4 12.1 1.0 CA B:PHE210 4.4 12.2 1.0 N B:ASP213 4.6 10.8 1.0 OG B:SER207 4.6 14.3 1.0 CB B:ASP213 4.7 11.5 1.0 CB B:ALA151 4.7 12.1 1.0 O B:TRP258 4.8 9.8 1.0 N B:VAL261 4.8 12.9 1.0 O B:HOH770 4.9 21.0 1.0 CG B:ASP259 4.9 15.0 1.0

D.Mandelman, A.Belaich, J.P.Belaich, N.Aghajari, H.Driguez, R.Haser. X-Ray Crystal Structure of the Multidomain Endoglucanase CEL9G From Clostridium Cellulolyticum Complexed with Natural and Synthetic Cello-Oligosaccharides J.Bacteriol. V. 185 4127 2003.
ISSN: ISSN 0021-9193
PubMed: 12837787
DOI: 10.1128/JB.185.14.4127-4135.2003