Zinc in PDB 6vji: Structure of Mammalian NEIL2 From Monodelphis Domestica

The structure of Structure of Mammalian NEIL2 From Monodelphis Domestica, PDB code: 6vji was solved by B.E.Eckenroth, S.Doublie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.96 / 2.54
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	67.887, 67.887, 149.130, 90.00, 90.00, 120.00
R / Rfree (%)	25 / 27.5

The binding sites of Zinc atom in the Structure of Mammalian NEIL2 From Monodelphis Domestica (pdb code 6vji). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Mammalian NEIL2 From Monodelphis Domestica, PDB code: 6vji:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Mammalian NEIL2 From Monodelphis Domestica


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Mammalian NEIL2 From Monodelphis Domestica within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:0.6 occ:1.00 ND1 A:HIS298 2.0 0.2 1.0 SG A:CYS318 2.3 0.5 1.0 SG A:CYS294 2.3 0.6 1.0 SG A:CYS321 2.3 97.9 1.0 CG A:HIS298 2.9 0.2 1.0 CE1 A:HIS298 3.1 0.8 1.0 CB A:HIS298 3.2 0.3 1.0 CB A:CYS294 3.2 0.6 1.0 CB A:CYS318 3.6 0.4 1.0 CB A:CYS321 3.7 0.1 1.0 N A:HIS298 3.9 0.7 1.0 CB A:ALA296 4.0 0.3 1.0 N A:CYS321 4.1 0.6 1.0 CA A:HIS298 4.1 0.4 1.0 CD2 A:HIS298 4.1 0.6 1.0 NE2 A:HIS298 4.1 0.7 1.0 CA A:CYS321 4.5 0.0 1.0 CB A:HIS320 4.6 0.3 1.0 O A:HIS298 4.6 0.9 1.0 CA A:CYS294 4.7 0.8 1.0 N A:GLY297 4.7 0.6 1.0 C A:HIS298 4.7 0.1 1.0 N A:ALA296 4.8 0.3 1.0 CA A:ALA296 4.9 0.3 1.0 CA A:CYS318 4.9 1.0 1.0 C A:HIS320 5.0 0.3 1.0

Zinc binding site 2 out of 2 in the Structure of Mammalian NEIL2 From Monodelphis Domestica


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Mammalian NEIL2 From Monodelphis Domestica within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:0.1 occ:1.00 ND1 B:HIS298 2.0 0.5 1.0 SG B:CYS294 2.3 0.7 1.0 SG B:CYS318 2.3 0.9 1.0 SG B:CYS321 2.3 94.8 1.0 CG B:HIS298 2.9 0.0 1.0 CB B:HIS298 3.0 0.9 1.0 CE1 B:HIS298 3.1 0.7 1.0 CB B:CYS294 3.1 0.5 1.0 CB B:CYS318 3.7 0.4 1.0 CB B:CYS321 3.7 0.0 1.0 N B:HIS298 3.9 0.6 1.0 N B:CYS321 4.0 0.7 1.0 CA B:HIS298 4.0 0.1 1.0 CD2 B:HIS298 4.1 0.4 1.0 NE2 B:HIS298 4.2 0.0 1.0 CB B:HIS320 4.4 0.8 1.0 CB B:ALA296 4.4 0.1 1.0 CA B:CYS321 4.4 0.4 1.0 O B:HIS298 4.4 0.8 1.0 CA B:CYS294 4.6 0.7 1.0 C B:HIS298 4.6 0.8 1.0 C B:HIS320 4.8 0.9 1.0 N B:GLY297 4.8 0.9 1.0 N B:CYS294 5.0 0.9 1.0 CA B:CYS318 5.0 0.0 1.0

B.E.Eckenroth, V.B.Cao, A.M.Averill, J.A.Dragon, S.Doublie. Unique Structural Features of Mammalian NEIL2 Dna Glycosylase Prime Its Activity For Diverse Dna Substrates and Environments. Structure 2020.
ISSN: ISSN 0969-2126
PubMed: 32846144
DOI: 10.1016/J.STR.2020.08.001