Zinc in PDB 8pn3: Crystal Structure of the HC7-GLU200ALA Mutant Complexed to A Tetraglycopeptide.

The structure of Crystal Structure of the HC7-GLU200ALA Mutant Complexed to A Tetraglycopeptide., PDB code: 8pn3 was solved by V.Taleb, R.Hurtado-Guerrero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.90 / 1.44
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	84.703, 91.94, 99.741, 90, 90, 90
R / Rfree (%)	17 / 20.1

The binding sites of Zinc atom in the Crystal Structure of the HC7-GLU200ALA Mutant Complexed to A Tetraglycopeptide. (pdb code 8pn3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the HC7-GLU200ALA Mutant Complexed to A Tetraglycopeptide., PDB code: 8pn3:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of the HC7-GLU200ALA Mutant Complexed to A Tetraglycopeptide.


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 the HC7-GLU200ALA Mutant Complexed to A Tetraglycopeptide. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn702 b:13.1 occ:1.00 O A:HOH953 1.8 15.7 1.0 OE1 A:GLU112 1.9 11.9 1.0 NE2 A:HIS161 2.0 10.9 1.0 CD A:GLU112 2.8 10.8 1.0 CE1 A:HIS161 2.9 12.8 1.0 OE2 A:GLU112 3.0 12.6 1.0 CD2 A:HIS161 3.2 12.4 1.0 O A:HOH834 4.0 21.9 1.0 ND1 A:HIS161 4.1 13.3 1.0 O A:HOH928 4.1 17.2 1.0 CB A:PRO185 4.2 13.4 1.0 CG A:HIS161 4.2 11.8 1.0 CG A:GLU112 4.2 12.5 1.0 CA A:PRO185 4.6 14.5 1.0 O A:PRO185 4.7 16.7 1.0 CB A:GLU112 4.7 14.0 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of the HC7-GLU200ALA Mutant Complexed to A Tetraglycopeptide.


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 the HC7-GLU200ALA Mutant Complexed to A Tetraglycopeptide. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn703 b:15.2 occ:1.00 OE2 A:GLU318 1.9 15.3 1.0 CD A:GLU318 2.8 16.2 1.0 O A:HOH1073 2.9 17.6 1.0 OE1 A:GLU318 2.9 15.9 1.0 NZ A:LYS316 3.7 15.1 1.0 NZ A:LYS356 4.0 16.1 1.0 CG A:GLU318 4.2 13.4 1.0 O A:HOH1116 4.2 24.6 1.0 OH A:TYR320 4.3 17.5 1.0 O A:HOH945 4.5 17.5 1.0 CE A:LYS316 4.7 15.9 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of the HC7-GLU200ALA Mutant Complexed to A Tetraglycopeptide.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the HC7-GLU200ALA Mutant Complexed to A Tetraglycopeptide. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn704 b:17.8 occ:1.00 OE2 A:GLU158 2.0 18.6 1.0 NZ A:LYS337 2.0 19.9 1.0 OD1 A:ASP335 2.1 16.7 1.0 CD A:GLU158 2.7 17.4 1.0 OE1 A:GLU158 2.8 17.6 1.0 CG A:ASP335 2.9 19.3 1.0 O A:HOH1105 2.9 26.4 1.0 OD2 A:ASP335 3.0 22.2 1.0 CE A:LYS337 3.0 18.6 1.0 CD A:LYS337 3.4 16.6 1.0 O A:HOH807 3.8 35.3 1.0 O A:HOH847 3.9 22.5 1.0 O A:HOH884 4.1 32.3 1.0 O A:HOH1088 4.1 37.2 1.0 CG A:GLU158 4.1 16.9 1.0 CB A:ASP335 4.3 16.6 1.0 O A:HOH1126 4.3 33.7 1.0 O A:HOH801 4.6 20.7 1.0 O A:ASP335 4.7 14.9 1.0 CG A:LYS337 4.8 14.7 1.0 CA A:ASP335 4.8 15.9 1.0

Y.Narimatsu, C.Bull, V.Taleb, Q.Liao, I.Companon, D.Sanchez-Navarro, F.Durbesson, R.Vincentelli, L.Hansen, F.Corzana, C.Rovira, B.Henrissat, H.Clausen, H.J.Joshi, R.Hurtado-Guerrero. A Family of Di-Glutamate Mucin-Degrading Enzymes That Bridges Glycan Hydrolases and Peptidases Nat Catal 2024.
ISSN: ESSN 2520-1158
DOI: 10.1038/S41929-024-01116-5