Zinc in PDB 4fvb: Crystal Structure of EV71 2A Proteinase C110A Mutant

All present enzymatic activity of Crystal Structure of EV71 2A Proteinase C110A Mutant:
3.4.22.29;

The structure of Crystal Structure of EV71 2A Proteinase C110A Mutant, PDB code: 4fvb was solved by Q.Cai, Y.Muhammad, W.Liu, Z.Gao, X.Peng, Y.Cai, C.Wu, Q.Zheng, J.Li, T.Lin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	86.613, 44.265, 52.036, 90.00, 112.58, 90.00
R / Rfree (%)	19.5 / 23.9

The binding sites of Zinc atom in the Crystal Structure of EV71 2A Proteinase C110A Mutant (pdb code 4fvb). 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 EV71 2A Proteinase C110A Mutant, PDB code: 4fvb:

Zinc binding site 1 out of 1 in the Crystal Structure of EV71 2A Proteinase C110A Mutant


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 EV71 2A Proteinase C110A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:38.0 occ:1.00 ND1 A:HIS118 2.2 40.4 1.0 SG A:CYS58 2.2 34.4 1.0 SG A:CYS116 2.2 30.8 1.0 SG A:CYS56 2.4 33.5 1.0 CB A:CYS58 3.1 32.7 1.0 CE1 A:HIS118 3.1 38.4 1.0 CG A:HIS118 3.2 41.3 1.0 CB A:CYS56 3.3 25.3 1.0 CB A:CYS116 3.4 26.2 1.0 CB A:HIS118 3.5 32.6 1.0 N A:HIS118 3.8 36.1 1.0 N A:CYS58 4.2 27.6 1.0 CA A:CYS58 4.2 29.2 1.0 CA A:HIS118 4.2 31.9 1.0 NE2 A:HIS118 4.2 46.5 1.0 CD2 A:HIS118 4.3 41.4 1.0 CB A:ALA54 4.3 22.4 1.0 CG A:GLN117 4.4 38.5 1.0 N A:GLN117 4.5 30.7 1.0 CA A:CYS116 4.6 28.4 1.0 O A:HOH382 4.6 38.4 1.0 C A:CYS116 4.7 24.7 1.0 CA A:CYS56 4.8 26.4 1.0 CG2 A:VAL121 4.9 24.3 1.0 O A:HOH405 4.9 41.5 1.0 C A:GLN117 5.0 38.5 1.0

Q.Cai, M.Yameen, W.Liu, Z.Gao, Y.Li, X.Peng, Y.Cai, C.Wu, Q.Zheng, J.Li, T.Lin. Conformational Plasticity of 2A Proteinase From Enterovirus 71 J.Virol. V. 87 7348 2013.
ISSN: ISSN 0022-538X
PubMed: 23616646
DOI: 10.1128/JVI.03541-12