Zinc in PDB 8qxz: Xylanase From Bacillus Circulans Mutant E78Q/Y69A

The structure of Xylanase From Bacillus Circulans Mutant E78Q/Y69A, PDB code: 8qxz 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)	68.26 / 1.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	79.345, 79.345, 133.171, 90, 90, 90
R / Rfree (%)	15.4 / 18.3

The binding sites of Zinc atom in the Xylanase From Bacillus Circulans Mutant E78Q/Y69A (pdb code 8qxz). 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/Y69A, PDB code: 8qxz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Xylanase From Bacillus Circulans Mutant E78Q/Y69A


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/Y69A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:17.7 occ:1.00 NE2 A:HIS156 2.0 17.3 1.0 N A:BTB202 2.1 20.1 1.0 O6 A:BTB202 2.1 15.5 1.0 O8 A:BTB202 2.2 17.1 1.0 O4 A:BTB202 2.2 18.3 1.0 O3 A:BTB202 2.2 18.8 1.0 C2 A:BTB202 2.8 19.6 1.0 C5 A:BTB202 2.9 20.4 1.0 C6 A:BTB202 2.9 17.4 1.0 CD2 A:HIS156 2.9 17.0 1.0 C4 A:BTB202 3.0 22.0 1.0 C3 A:BTB202 3.0 21.4 1.0 C8 A:BTB202 3.0 19.3 1.0 CE1 A:HIS156 3.0 17.8 1.0 C7 A:BTB202 3.1 20.3 1.0 O A:THR97 3.9 18.2 1.0 CG A:HIS156 4.1 17.5 1.0 ND1 A:HIS156 4.1 20.0 1.0 O A:HOH317 4.2 28.6 1.0 OG A:SER155 4.2 28.6 1.0 C1 A:BTB202 4.3 22.4 1.0 N A:THR97 4.8 15.2 1.0 O1 A:BTB202 4.9 24.6 1.0

Zinc binding site 2 out of 2 in the Xylanase From Bacillus Circulans Mutant E78Q/Y69A


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/Y69A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:17.3 occ:1.00 NE2 B:HIS156 2.0 17.8 1.0 N B:BTB202 2.1 18.4 1.0 O6 B:BTB202 2.2 16.5 1.0 O8 B:BTB202 2.2 16.2 1.0 O4 B:BTB202 2.2 17.9 1.0 O1 B:BTB202 2.2 17.2 1.0 C2 B:BTB202 2.8 18.5 1.0 C6 B:BTB202 2.9 17.9 1.0 C4 B:BTB202 2.9 17.3 1.0 C5 B:BTB202 2.9 20.1 1.0 CD2 B:HIS156 3.0 17.0 1.0 C8 B:BTB202 3.0 17.4 1.0 C1 B:BTB202 3.0 17.3 1.0 CE1 B:HIS156 3.0 18.9 1.0 C7 B:BTB202 3.0 18.7 1.0 O B:THR97 3.9 17.7 1.0 O B:HOH308 4.0 27.6 1.0 CG B:HIS156 4.1 18.3 1.0 ND1 B:HIS156 4.1 19.9 1.0 C3 B:BTB202 4.3 24.7 1.0 OG B:SER155 4.3 29.3 1.0 N B:THR97 4.8 15.6 1.0 O3 B:BTB202 4.9 27.7 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