Zinc in PDB 8qxy: Xylanase From Bacillus Circulans Mutant E78Q Bound to Xylotriose

The structure of Xylanase From Bacillus Circulans Mutant E78Q Bound to Xylotriose, PDB code: 8qxy was solved by A.Chikunova, M.Saberi, M.Ubbink, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.29 / 1.41
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.32, 80.32, 133.48, 90, 90, 90
R / Rfree (%)	18.4 / 21.1

The binding sites of Zinc atom in the Xylanase From Bacillus Circulans Mutant E78Q Bound to Xylotriose (pdb code 8qxy). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Xylanase From Bacillus Circulans Mutant E78Q Bound to Xylotriose, PDB code: 8qxy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Xylanase From Bacillus Circulans Mutant E78Q Bound to Xylotriose


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Xylanase From Bacillus Circulans Mutant E78Q Bound to Xylotriose within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:20.3 occ:1.00 NE2 A:HIS156 2.0 20.3 1.0 N A:BTB202 2.1 22.7 1.0 O3 A:BTB202 2.1 20.2 1.0 O6 A:BTB202 2.2 19.2 1.0 O8 A:BTB202 2.2 18.9 1.0 O4 A:BTB202 2.2 21.7 1.0 C2 A:BTB202 2.8 23.1 1.0 C7 A:BTB202 2.9 21.6 1.0 C8 A:BTB202 2.9 19.8 1.0 CD2 A:HIS156 2.9 21.7 1.0 C4 A:BTB202 2.9 22.4 1.0 C3 A:BTB202 3.0 21.2 1.0 C6 A:BTB202 3.0 24.1 1.0 C5 A:BTB202 3.0 23.4 1.0 CE1 A:HIS156 3.1 21.8 1.0 O A:THR97 3.9 21.4 1.0 O A:HOH306 4.0 29.2 1.0 CG A:HIS156 4.1 21.4 1.0 ND1 A:HIS156 4.1 21.2 1.0 OG A:SER155 4.2 28.8 1.0 C1 A:BTB202 4.3 28.4 1.0 N A:THR97 4.7 18.0 1.0 O A:HOH429 4.8 41.8 1.0 O1 A:BTB202 5.0 34.1 1.0

Zinc binding site 2 out of 2 in the Xylanase From Bacillus Circulans Mutant E78Q Bound to Xylotriose


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Xylanase From Bacillus Circulans Mutant E78Q Bound to Xylotriose within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:19.1 occ:1.00 NE2 B:HIS156 2.0 21.3 1.0 O6 B:BTB202 2.1 17.9 1.0 N B:BTB202 2.1 19.3 1.0 O8 B:BTB202 2.1 18.2 1.0 O1 B:BTB202 2.2 18.6 1.0 O3 B:BTB202 2.2 16.5 1.0 C2 B:BTB202 2.7 20.0 1.0 CD2 B:HIS156 2.9 20.8 1.0 C3 B:BTB202 2.9 20.9 1.0 C1 B:BTB202 2.9 18.7 1.0 C6 B:BTB202 2.9 19.2 1.0 C5 B:BTB202 3.0 19.6 1.0 C8 B:BTB202 3.0 19.9 1.0 CE1 B:HIS156 3.0 23.1 1.0 C7 B:BTB202 3.1 18.9 1.0 O B:THR97 3.9 18.6 1.0 O B:HOH309 4.0 33.8 1.0 CG B:HIS156 4.1 21.3 1.0 ND1 B:HIS156 4.1 23.2 1.0 C4 B:BTB202 4.2 25.5 1.0 OG B:SER155 4.3 26.4 1.0 N B:THR97 4.8 17.2 1.0 O4 B:BTB202 4.9 26.1 1.0

M.Saberi, A.Chikunova, M.Ubbink. Bimodal Substrate Binding in the Active Site of the Glycosidase Bcx Febs J. 2024.
ISSN: ISSN 1742-464X
DOI: 10.1111/FEBS.17251