Zinc in PDB 7ojj: Lassa Virus L Protein with Endonuclease and C-Terminal Domains in Close Proximity [Mid-Link]

All present enzymatic activity of Lassa Virus L Protein with Endonuclease and C-Terminal Domains in Close Proximity [Mid-Link]:
2.7.7.48;

The structure of Lassa Virus L Protein with Endonuclease and C-Terminal Domains in Close Proximity [Mid-Link] also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Lassa Virus L Protein with Endonuclease and C-Terminal Domains in Close Proximity [Mid-Link] (pdb code 7ojj). 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 Lassa Virus L Protein with Endonuclease and C-Terminal Domains in Close Proximity [Mid-Link], PDB code: 7ojj:

Zinc binding site 1 out of 1 in the Lassa Virus L Protein with Endonuclease and C-Terminal Domains in Close Proximity [Mid-Link]


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Lassa Virus L Protein with Endonuclease and C-Terminal Domains in Close Proximity [Mid-Link] within 5.0Å range: probe atom residue distance (Å) B Occ L:Zn2301 b:217.2 occ:1.00 O L:LYS319 2.3 209.7 1.0 NE2 L:HIS316 2.5 207.5 1.0 CE1 L:HIS316 2.9 207.5 1.0 SG L:CYS366 3.1 208.4 1.0 SG L:CYS321 3.3 206.7 1.0 CD2 L:HIS316 3.4 207.5 1.0 C L:LYS319 3.5 209.7 1.0 CD2 L:HIS364 3.7 216.2 1.0 CB L:CYS366 3.7 208.4 1.0 ND1 L:HIS316 3.9 207.5 1.0 NE2 L:HIS364 4.0 216.2 1.0 CG L:HIS316 4.2 207.5 1.0 CB L:LYS319 4.2 209.7 1.0 C L:GLU320 4.3 204.4 1.0 N L:CYS321 4.3 206.7 1.0 O L:HIS316 4.4 207.5 1.0 N L:GLU320 4.4 204.4 1.0 CA L:LYS319 4.4 209.7 1.0 CA L:GLU320 4.5 204.4 1.0 CG L:HIS364 4.6 216.2 1.0 O L:GLU320 4.6 204.4 1.0 CB L:CYS321 4.7 206.7 1.0 CA L:CYS321 4.8 206.7 1.0 NZ L:LYS368 4.9 188.2 1.0

T.Kouba, D.Vogel, S.Thorkelsson, E.Quemin, H.William, M.Milewski, C.Busch, S.Gunther, K.Grunewald, M.Rosenthal, S.Cusack. Conformational Changes in Lassa Virus L Protein Associated with Promoter Binding and Rna Synthesis Activity To Be Published.