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Zinc in PDB 5f8l: Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)

Enzymatic activity of Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)

All present enzymatic activity of Enterovirus 71 Polymerase Elongation Complex (C3S1 Form):
2.7.7.48;

Protein crystallography data

The structure of Enterovirus 71 Polymerase Elongation Complex (C3S1 Form), PDB code: 5f8l was solved by B.Shu, P.Gong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.03 / 2.81
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.228, 76.709, 151.247, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 23.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Enterovirus 71 Polymerase Elongation Complex (C3S1 Form) (pdb code 5f8l). 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 Enterovirus 71 Polymerase Elongation Complex (C3S1 Form), PDB code: 5f8l:

Zinc binding site 1 out of 1 in 5f8l

Go back to Zinc Binding Sites List in 5f8l
Zinc binding site 1 out of 1 in the Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Enterovirus 71 Polymerase Elongation Complex (C3S1 Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2001

b:46.9
occ:0.71
NE2 A:HIS271 1.9 48.7 1.0
NE2 A:HIS273 2.0 52.8 1.0
SG A:CYS282 2.1 48.9 1.0
CD2 A:HIS273 2.7 51.1 1.0
CE1 A:HIS271 2.9 53.2 1.0
CD2 A:HIS271 2.9 49.8 1.0
CB A:CYS282 3.1 56.5 1.0
CE1 A:HIS273 3.2 53.6 1.0
NE1 A:TRP5 3.8 55.0 1.0
ND1 A:HIS271 4.0 55.4 1.0
CG A:HIS273 4.0 52.0 1.0
CG A:HIS271 4.0 54.6 1.0
ND1 A:HIS273 4.2 50.7 1.0
CZ2 A:TRP5 4.2 52.4 1.0
CA A:CYS282 4.2 53.9 1.0
CE2 A:TRP5 4.3 57.0 1.0
O A:THR272 4.5 55.0 1.0
CD1 A:TRP5 4.9 57.8 1.0
C A:CYS282 4.9 50.7 1.0

Reference:

B.Shu, P.Gong. Structural Basis of Viral Rna-Dependent Rna Polymerase Catalysis and Translocation Proc.Natl.Acad.Sci.Usa V. 113 E4005 2016.
ISSN: ESSN 1091-6490
PubMed: 27339134
DOI: 10.1073/PNAS.1602591113
Page generated: Wed Dec 16 06:13:16 2020

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