Zinc in PDB 6jea: Crystal Structure of A Beta-N-Acetylhexosaminidase

All present enzymatic activity of Crystal Structure of A Beta-N-Acetylhexosaminidase:
3.2.1.52;

The structure of Crystal Structure of A Beta-N-Acetylhexosaminidase, PDB code: 6jea was solved by X.Chen, J.C.Wang, M.J.Liu, W.Y.Yang, Y.Z.Wang, R.P.Tang, M.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.01 / 2.28
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.555, 83.309, 91.350, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 21.5

The binding sites of Zinc atom in the Crystal Structure of A Beta-N-Acetylhexosaminidase (pdb code 6jea). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of A Beta-N-Acetylhexosaminidase, PDB code: 6jea:

Zinc binding site 1 out of 1 in the Crystal Structure of A Beta-N-Acetylhexosaminidase


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 A Beta-N-Acetylhexosaminidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:28.4 occ:1.00 SG A:CYS288 2.4 25.7 1.0 SG A:CYS227 2.4 32.1 1.0 SG A:CYS291 2.4 32.5 1.0 SG A:CYS247 2.4 26.1 1.0 CB A:CYS288 3.1 26.5 1.0 CB A:CYS247 3.3 28.7 1.0 CB A:CYS227 3.5 28.4 1.0 CB A:CYS291 3.6 28.7 1.0 CA A:CYS247 3.8 27.2 1.0 N A:CYS291 3.9 26.9 1.0 CA A:CYS227 4.1 31.0 1.0 CA A:CYS291 4.3 29.6 1.0 CD A:PRO248 4.4 27.5 1.0 CD1 A:TRP285 4.4 28.1 1.0 CB A:LEU290 4.5 26.6 1.0 CG A:GLN249 4.5 27.2 1.0 CA A:CYS288 4.6 28.1 1.0 C A:CYS247 4.6 27.0 1.0 O A:HOH858 4.6 34.3 1.0 N A:CYS227 4.7 27.5 1.0 N A:PRO248 4.8 28.1 1.0 NE1 A:TRP285 4.9 29.4 1.0 C A:LEU290 4.9 26.2 1.0 N A:CYS247 5.0 28.2 1.0

X.Chen, J.Wang, M.Liu, W.Yang, Y.Wang, R.Tang, M.Zhang. Crystallographic Evidence For Substrate-Assisted Catalysis of Beta-N-Acetylhexosaminidas From Akkermansia Muciniphila. Biochem. Biophys. Res. V. 511 833 2019COMMUN..
ISSN: ESSN 1090-2104
PubMed: 30846208
DOI: 10.1016/J.BBRC.2019.02.074