Zinc in PDB 4gl2: Structural Basis For Dsrna Duplex Backbone Recognition By MDA5

All present enzymatic activity of Structural Basis For Dsrna Duplex Backbone Recognition By MDA5:
3.6.4.13;

The structure of Structural Basis For Dsrna Duplex Backbone Recognition By MDA5, PDB code: 4gl2 was solved by B.Wu, S.Hur, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	118.70 / 3.56
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.112, 154.748, 185.006, 90.00, 90.00, 90.00
R / Rfree (%)	27.6 / 32

The binding sites of Zinc atom in the Structural Basis For Dsrna Duplex Backbone Recognition By MDA5 (pdb code 4gl2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structural Basis For Dsrna Duplex Backbone Recognition By MDA5, PDB code: 4gl2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structural Basis For Dsrna Duplex Backbone Recognition By MDA5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis For Dsrna Duplex Backbone Recognition By MDA5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1102 b:53.6 occ:1.00 SG A:CYS964 2.2 0.4 1.0 SG A:CYS962 2.3 70.7 1.0 SG A:CYS907 2.4 42.9 1.0 SG A:CYS910 2.5 47.7 1.0 HB3 A:CYS907 2.9 60.5 1.0 HB3 A:CYS910 3.0 89.7 1.0 CB A:CYS907 3.1 50.4 1.0 HB2 A:CYS907 3.2 60.5 1.0 HG12 A:VAL912 3.2 67.2 1.0 CB A:CYS910 3.3 74.7 1.0 H A:CYS910 3.5 98.5 1.0 HZ2 A:TRP968 3.6 58.6 1.0 HG11 A:VAL912 3.6 67.2 1.0 CB A:CYS962 3.7 50.0 1.0 H A:CYS964 3.7 81.1 1.0 HE1 A:TRP968 3.7 55.0 1.0 O A:CYS910 3.8 76.4 1.0 CB A:CYS964 3.8 69.4 1.0 HB2 A:CYS962 3.8 60.0 1.0 CG1 A:VAL912 3.8 56.0 1.0 HB3 A:CYS962 3.9 60.0 1.0 HB2 A:CYS964 3.9 83.2 1.0 N A:CYS910 4.0 82.1 1.0 HB3 A:ASN909 4.0 0.9 1.0 CA A:CYS910 4.1 77.6 1.0 HB2 A:CYS910 4.1 89.7 1.0 C A:CYS910 4.2 74.9 1.0 HB3 A:CYS964 4.3 83.2 1.0 CZ2 A:TRP968 4.4 48.8 1.0 HG13 A:VAL912 4.4 67.2 1.0 NE1 A:TRP968 4.4 45.9 1.0 HB3 A:GLN966 4.5 89.1 1.0 N A:CYS964 4.5 67.6 1.0 CA A:CYS907 4.5 51.8 1.0 H A:LYS963 4.7 59.5 1.0 HB A:VAL912 4.7 70.9 1.0 CE2 A:TRP968 4.7 46.3 1.0 CA A:CYS964 4.8 70.2 1.0 CB A:ASN909 5.0 92.4 1.0 CB A:VAL912 5.0 59.1 1.0 HA A:CYS910 5.0 93.1 1.0

Zinc binding site 2 out of 2 in the Structural Basis For Dsrna Duplex Backbone Recognition By MDA5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Basis For Dsrna Duplex Backbone Recognition By MDA5 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1102 b:41.2 occ:1.00 SG B:CYS910 2.3 61.8 1.0 SG B:CYS962 2.4 45.4 1.0 SG B:CYS964 2.4 87.5 1.0 SG B:CYS907 2.4 0.6 1.0 HB3 B:CYS910 2.5 89.1 1.0 HB3 B:CYS964 2.7 86.1 1.0 CB B:CYS910 2.9 74.3 1.0 CB B:CYS964 3.1 71.7 1.0 H B:CYS964 3.1 73.9 1.0 O B:ASN909 3.2 78.4 1.0 HB3 B:CYS962 3.4 50.1 1.0 HG12 B:VAL912 3.5 56.9 1.0 HB2 B:CYS910 3.5 89.1 1.0 CB B:CYS962 3.5 41.8 1.0 HB2 B:CYS962 3.7 50.1 1.0 HB2 B:CYS964 3.8 86.1 1.0 N B:CYS964 3.9 61.6 1.0 C B:ASN909 3.9 79.6 1.0 CB B:CYS907 3.9 75.9 1.0 HB3 B:CYS907 4.0 91.1 1.0 HB3 B:ASN909 4.1 91.0 1.0 HE1 B:TRP968 4.1 77.7 1.0 CA B:CYS964 4.1 69.4 1.0 CA B:CYS910 4.1 80.2 1.0 HB3 B:GLN966 4.2 77.6 1.0 HB2 B:CYS907 4.2 91.1 1.0 HG11 B:VAL912 4.2 56.9 1.0 HZ2 B:TRP968 4.2 75.9 1.0 CG1 B:VAL912 4.3 47.4 1.0 H B:LYS963 4.3 58.1 1.0 N B:CYS910 4.3 82.7 1.0 HB2 B:LYS963 4.4 67.7 1.0 H B:GLN966 4.5 84.0 1.0 C B:CYS910 4.6 66.5 1.0 N B:LYS963 4.7 48.4 1.0 NE1 B:TRP968 4.8 64.7 1.0 H B:GLY965 4.8 83.9 1.0 H B:VAL912 4.8 69.9 1.0 H B:ASN909 4.8 86.6 1.0 HA B:CYS964 4.8 83.3 1.0 HG13 B:VAL912 4.8 56.9 1.0 CA B:CYS962 4.9 41.0 1.0 HA B:CYS910 4.9 96.2 1.0 CB B:ASN909 4.9 75.8 1.0 HB2 B:GLN966 4.9 77.6 1.0 CZ2 B:TRP968 4.9 63.2 1.0 CA B:ASN909 4.9 76.2 1.0 H B:SER911 4.9 70.7 1.0 HB B:VAL912 5.0 58.8 1.0 N B:SER911 5.0 59.0 1.0 CB B:GLN966 5.0 64.7 1.0

B.Wu, A.Peisley, C.Richards, H.Yao, X.Zeng, C.Lin, F.Chu, T.Walz, S.Hur. Structural Basis For Dsrna Recognition, Filament Formation, and Antiviral Signal Activation By MDA5. Cell(Cambridge,Mass.) V. 152 276 2013.
ISSN: ISSN 0092-8674
PubMed: 23273991
DOI: 10.1016/J.CELL.2012.11.048