Zinc in PDB 4mg3: Crystal Structural Analysis of 2A Protease From Coxsackievirus A16

All present enzymatic activity of Crystal Structural Analysis of 2A Protease From Coxsackievirus A16:
3.4.22.29;

The structure of Crystal Structural Analysis of 2A Protease From Coxsackievirus A16, PDB code: 4mg3 was solved by Y.Sun, X.Wang, M.Dang, S.Yuan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.47 / 1.80
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	101.271, 101.271, 193.914, 90.00, 90.00, 120.00
R / Rfree (%)	17.3 / 20.3

The binding sites of Zinc atom in the Crystal Structural Analysis of 2A Protease From Coxsackievirus A16 (pdb code 4mg3). 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 Structural Analysis of 2A Protease From Coxsackievirus A16, PDB code: 4mg3:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structural Analysis of 2A Protease From Coxsackievirus A16


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structural Analysis of 2A Protease From Coxsackievirus A16 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:32.7 occ:1.00 ND1 A:HIS118 2.2 31.6 1.0 SG A:CYS56 2.2 35.2 1.0 SG A:CYS116 2.4 25.9 1.0 SG A:CYS58 2.4 35.1 1.0 CB A:CYS58 3.0 37.4 1.0 CE1 A:HIS118 3.1 38.5 1.0 CB A:CYS56 3.1 38.6 1.0 CG A:HIS118 3.1 35.8 1.0 CB A:CYS116 3.4 22.6 1.0 CB A:HIS118 3.4 32.0 1.0 N A:HIS118 3.9 29.9 1.0 CA A:CYS58 4.2 33.4 1.0 N A:CYS58 4.2 32.2 1.0 NE2 A:HIS118 4.2 36.3 1.0 CD2 A:HIS118 4.3 40.8 1.0 CA A:HIS118 4.3 28.7 1.0 CA A:CYS56 4.5 39.6 1.0 CB A:ALA54 4.5 25.6 1.0 N A:GLN117 4.6 32.2 1.0 CA A:CYS116 4.7 26.8 1.0 CG A:GLN117 4.7 57.3 1.0 C A:CYS116 4.8 27.1 1.0 O A:HOH414 4.8 44.5 1.0 N A:CYS56 4.9 46.6 1.0 O A:HOH401 5.0 41.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structural Analysis of 2A Protease From Coxsackievirus A16


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structural Analysis of 2A Protease From Coxsackievirus A16 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:29.6 occ:1.00 ND1 B:HIS118 2.2 25.5 1.0 SG B:CYS56 2.3 29.8 1.0 SG B:CYS116 2.3 23.5 1.0 SG B:CYS58 2.4 31.5 1.0 CG B:HIS118 3.1 31.1 1.0 CB B:CYS58 3.1 26.1 1.0 CE1 B:HIS118 3.1 34.3 1.0 CB B:CYS56 3.2 31.5 1.0 CB B:CYS116 3.3 23.9 1.0 CB B:HIS118 3.4 21.3 1.0 N B:HIS118 3.9 25.4 1.0 N B:CYS58 4.2 28.6 1.0 NE2 B:HIS118 4.3 34.0 1.0 CA B:HIS118 4.3 26.2 1.0 CD2 B:HIS118 4.3 34.5 1.0 CA B:CYS58 4.3 28.0 1.0 CG B:GLN117 4.5 53.6 1.0 CB B:ALA54 4.5 20.3 1.0 N B:GLN117 4.5 26.3 1.0 CA B:CYS56 4.6 25.7 1.0 CA B:CYS116 4.6 21.4 1.0 C B:CYS116 4.8 21.9 1.0 N B:CYS56 5.0 35.0 1.0

Y.Sun, X.Wang, S.Yuan, M.Dang, X.Li, X.C.Zhang, Z.Rao. An Open Conformation Determined By A Structural Switch For 2A Protease From Coxsackievirus A16. Protein Cell V. 4 782 2013.
ISSN: ISSN 1674-800X
PubMed: 24026848
DOI: 10.1007/S13238-013-3914-Z