Zinc in PDB 7vi8: Crystal Structure of Chbg

All present enzymatic activity of Crystal Structure of Chbg:
3.5.1.105;

The structure of Crystal Structure of Chbg, PDB code: 7vi8 was solved by S.Y.Lee, H.H.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.51 / 1.83
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.23, 67.03, 146.4, 90, 90, 90
R / Rfree (%)	22 / 25.7

The binding sites of Zinc atom in the Crystal Structure of Chbg (pdb code 7vi8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Chbg, PDB code: 7vi8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Chbg


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Chbg within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:69.5 occ:1.00 NE2 A:HIS60 2.5 21.1 1.0 OD2 A:ASP10 2.7 28.2 1.0 OD1 A:ASP10 2.9 27.4 1.0 CG A:ASP10 3.1 19.9 1.0 ND1 A:HIS124 3.1 24.6 1.0 O A:HOH501 3.2 33.2 1.0 CE1 A:HIS60 3.3 22.9 1.0 CD2 A:HIS60 3.5 23.9 1.0 CA A:HIS124 3.7 22.1 1.0 CE1 A:HIS124 3.8 29.0 1.0 CG A:HIS124 3.8 25.2 1.0 CB A:ASP9 3.9 21.1 1.0 CB A:HIS124 4.1 24.6 1.0 NE2 A:HIS205 4.2 20.7 1.0 OD2 A:ASP9 4.2 20.9 1.0 N A:HIS125 4.2 20.2 1.0 CB A:ASP10 4.5 20.0 1.0 ND1 A:HIS60 4.5 22.9 1.0 C A:HIS124 4.6 23.0 1.0 CG A:ASP9 4.6 23.6 1.0 N A:HIS124 4.6 20.8 1.0 CG A:HIS60 4.6 20.1 1.0 O A:SER123 4.7 20.9 1.0 NE2 A:HIS124 4.7 31.9 1.0 N A:ASP10 4.7 19.3 1.0 CD2 A:HIS124 4.8 24.5 1.0 O A:HOH411 4.8 31.3 1.0 CD2 A:HIS205 4.9 20.4 1.0 CA A:ASP10 5.0 21.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Chbg


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Chbg within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:68.0 occ:1.00 NE2 B:HIS60 2.2 23.6 1.0 OD1 B:ASP10 2.4 28.6 1.0 ND1 B:HIS124 2.4 33.2 1.0 CD2 B:HIS60 3.2 23.4 1.0 CE1 B:HIS124 3.2 35.6 1.0 CE1 B:HIS60 3.3 23.0 1.0 CG B:ASP10 3.3 29.9 1.0 O B:HOH492 3.4 30.5 1.0 CG B:HIS124 3.6 27.7 1.0 OD2 B:ASP10 3.6 31.8 1.0 CA B:HIS124 3.8 26.2 1.0 O B:HOH430 3.8 32.6 1.0 CB B:ASP9 3.9 18.9 1.0 CB B:HIS124 4.0 24.5 1.0 NE2 B:HIS205 4.1 24.7 1.0 OD2 B:ASP9 4.2 24.1 1.0 CG B:HIS60 4.3 22.1 1.0 ND1 B:HIS60 4.3 24.4 1.0 NE2 B:HIS124 4.4 32.3 1.0 N B:ASP10 4.4 19.5 1.0 CB B:ASP10 4.5 22.2 1.0 N B:HIS125 4.6 23.5 1.0 CG B:ASP9 4.6 24.6 1.0 CD2 B:HIS124 4.6 31.1 1.0 O B:HOH418 4.6 28.0 1.0 CD2 B:HIS205 4.7 23.9 1.0 N B:HIS124 4.7 20.1 1.0 CA B:ASP10 4.7 18.7 1.0 C B:HIS124 4.8 23.5 1.0 O B:SER123 4.9 21.4 1.0 C B:ASP9 5.0 21.3 1.0

S.Y.Lee, B.D.Pardhe, T.J.Oh, H.H.Park. Crystal Structure of Chbg From Klebsiella Pneumoniae Reveals the Molecular Basis of Diacetylchitobiose Deacetylation. Commun Biol V. 5 862 2022.
ISSN: ESSN 2399-3642
PubMed: 36002585
DOI: 10.1038/S42003-022-03824-9