Zinc in PDB 6u1x: Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor (3.0 A Resolution)

All present enzymatic activity of Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor (3.0 A Resolution):
2.1.1.296; 2.1.1.56; 2.7.7.48; 2.7.7.88;

The binding sites of Zinc atom in the Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor (3.0 A Resolution) (pdb code 6u1x). 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 the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor (3.0 A Resolution), PDB code: 6u1x:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor (3.0 A Resolution)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor (3.0 A Resolution) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn3000 b:90.0 occ:1.00 OE2 A:GLU1108 2.0 65.2 1.0 SG A:CYS1299 2.3 71.7 1.0 SG A:CYS1081 2.3 67.1 1.0 SG A:CYS1302 2.3 71.7 1.0 HB3 A:CYS1302 2.8 71.7 1.0 HB3 A:CYS1299 2.9 71.7 1.0 CB A:CYS1302 3.1 71.7 1.0 CD A:GLU1108 3.2 65.2 1.0 CB A:CYS1299 3.2 71.7 1.0 H A:CYS1302 3.3 71.7 1.0 HA A:CYS1081 3.3 67.1 1.0 HG3 A:GLU1108 3.6 65.2 1.0 CB A:CYS1081 3.6 67.1 1.0 H A:SER1082 3.6 66.5 1.0 HB2 A:CYS1299 3.7 71.7 1.0 HB3 A:SER1301 3.7 70.2 1.0 N A:CYS1302 3.8 71.7 1.0 HB2 A:CYS1081 3.8 67.1 1.0 HB2 A:CYS1302 3.9 71.7 1.0 CG A:GLU1108 3.9 65.2 1.0 CA A:CYS1081 4.0 67.1 1.0 CA A:CYS1302 4.1 71.7 1.0 OE1 A:GLU1108 4.1 65.2 1.0 H A:ALA1083 4.1 68.5 1.0 O A:CYS1299 4.2 71.7 1.0 N A:SER1082 4.3 66.5 1.0 HB2 A:GLU1108 4.4 65.2 1.0 HB3 A:CYS1081 4.4 67.1 1.0 CA A:CYS1299 4.5 71.7 1.0 HA A:CYS1302 4.5 71.7 1.0 C A:CYS1299 4.6 71.7 1.0 H A:SER1301 4.6 70.2 1.0 C A:CYS1081 4.6 67.1 1.0 HA A:MET1109 4.6 66.5 1.0 CB A:SER1301 4.7 70.2 1.0 C A:SER1301 4.7 70.2 1.0 HG2 A:GLU1108 4.7 65.2 1.0 HB3 A:ALA1083 4.7 68.5 1.0 CB A:GLU1108 4.8 65.2 1.0 HA A:CYS1299 4.9 71.7 1.0 N A:ALA1083 5.0 68.5 1.0 N A:SER1301 5.0 70.2 1.0

Zinc binding site 2 out of 2 in the Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor (3.0 A Resolution)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor (3.0 A Resolution) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn3001 b:86.0 occ:1.00 ND1 A:HIS1294 2.0 65.2 1.0 NE2 A:HIS1296 2.0 66.4 1.0 SG A:CYS1123 2.2 75.8 1.0 SG A:CYS1120 2.3 74.3 1.0 HE1 A:HIS1296 2.6 66.4 1.0 CE1 A:HIS1296 2.6 66.4 1.0 CG A:HIS1294 3.0 65.2 1.0 CE1 A:HIS1294 3.0 65.2 1.0 HB3 A:HIS1294 3.1 65.2 1.0 HB2 A:HIS1294 3.1 65.2 1.0 HE1 A:HIS1294 3.2 65.2 1.0 CD2 A:HIS1296 3.3 66.4 1.0 CB A:HIS1294 3.3 65.2 1.0 HD2 A:HIS1296 3.7 66.4 1.0 CB A:CYS1123 3.7 75.8 1.0 CB A:CYS1120 3.8 74.3 1.0 HB2 A:CYS1123 3.8 75.8 1.0 HB3 A:CYS1120 3.9 74.3 1.0 ND1 A:HIS1296 3.9 66.4 1.0 NE2 A:HIS1294 4.1 65.2 1.0 CD2 A:HIS1294 4.1 65.2 1.0 HG2 A:PRO1122 4.1 73.4 1.0 CG A:HIS1296 4.2 66.4 1.0 H A:CYS1123 4.3 75.8 1.0 HB2 A:CYS1120 4.3 74.3 1.0 HA A:CYS1123 4.4 75.8 1.0 N A:CYS1123 4.4 75.8 1.0 HB3 A:CYS1123 4.4 75.8 1.0 O A:CYS1120 4.4 74.3 1.0 CA A:CYS1123 4.4 75.8 1.0 HZ3 A:LYS1116 4.5 66.6 1.0 HD1 A:HIS1296 4.6 66.4 1.0 HB2 A:HIS1114 4.6 65.8 1.0 CA A:HIS1294 4.8 65.2 1.0 HD3 A:LYS1116 4.8 66.6 1.0 HE2 A:HIS1294 4.9 65.2 1.0 HZ2 A:LYS1116 4.9 66.6 1.0 CA A:CYS1120 4.9 74.3 1.0 HD2 A:LYS1116 5.0 66.6 1.0 HD2 A:HIS1294 5.0 65.2 1.0

S.Jenni, L.M.Bloyet, R.Diaz-Avalos, B.Liang, S.P.J.Whelan, N.Grigorieff, S.C.Harrison. Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor. Cell Rep V. 30 53 2020.
ISSN: ESSN 2211-1247
PubMed: 31914397
DOI: 10.1016/J.CELREP.2019.12.024