Zinc in PDB 7orj: La Crosse Virus Polymerase at Transcription Capped Rna Cleavage Stage

All present enzymatic activity of La Crosse Virus Polymerase at Transcription Capped Rna Cleavage Stage:
2.7.7.48;

The binding sites of Zinc atom in the La Crosse Virus Polymerase at Transcription Capped Rna Cleavage Stage (pdb code 7orj). 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 La Crosse Virus Polymerase at Transcription Capped Rna Cleavage Stage, PDB code: 7orj:

Zinc binding site 1 out of 1 in the La Crosse Virus Polymerase at Transcription Capped Rna Cleavage Stage


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of La Crosse Virus Polymerase at Transcription Capped Rna Cleavage Stage within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2301 b:99.4 occ:1.00 SG A:CYS2064 2.2 83.0 1.0 OD1 A:ASP2178 2.2 91.8 1.0 NE2 A:HIS2169 2.2 85.3 1.0 NE2 A:HIS2182 2.4 97.8 1.0 CE1 A:HIS2169 2.8 85.3 1.0 N A:GLY2066 3.0 88.8 1.0 CE1 A:HIS2182 3.2 97.8 1.0 CG A:ASP2178 3.3 91.8 1.0 CD2 A:HIS2169 3.4 85.3 1.0 CD2 A:HIS2182 3.5 97.8 1.0 CA A:GLY2066 3.6 88.8 1.0 N A:SER2067 3.7 88.2 1.0 OD2 A:ASP2178 3.9 91.8 1.0 CB A:CYS2064 3.9 83.0 1.0 ND1 A:HIS2169 4.0 85.3 1.0 N A:GLU2065 4.0 84.7 1.0 C A:GLU2065 4.1 84.7 1.0 C A:GLY2066 4.1 88.8 1.0 O A:SER2067 4.2 88.2 1.0 CD1 A:ILE2173 4.2 84.9 1.0 CG A:HIS2169 4.3 85.3 1.0 ND1 A:HIS2182 4.4 97.8 1.0 CA A:GLU2065 4.4 84.7 1.0 CB A:ASP2178 4.4 91.8 1.0 CG1 A:ILE2173 4.4 84.9 1.0 C A:CYS2064 4.5 83.0 1.0 CG A:HIS2182 4.6 97.8 1.0 CD2 A:TYR2181 4.7 93.9 1.0 CA A:CYS2064 4.8 83.0 1.0 CA A:SER2067 4.8 88.2 1.0 O A:ASP2178 5.0 91.8 1.0 C A:SER2067 5.0 88.2 1.0

B.Arragain, Q.Durieux Trouilleton, F.Baudin, J.Provaznik, N.Azevedo, S.Cusack, G.Schoehn, H.Malet. Structural Snapshots of La Crosse Virus Polymerase Reveal the Mechanisms Underlying Peribunyaviridae Replication and Transcription. Nat Commun V. 13 902 2022.
ISSN: ESSN 2041-1723
PubMed: 35173159
DOI: 10.1038/S41467-022-28428-Z