Zinc in PDB 9iv9: Cryo-Em Structure of A Truncated Nipah Virus L Protein Bound By Phosphoprotein Tetramer

All present enzymatic activity of Cryo-Em Structure of A Truncated Nipah Virus L Protein Bound By Phosphoprotein Tetramer:
2.1.1.375; 2.7.7.48; 2.7.7.88;

The binding sites of Zinc atom in the Cryo-Em Structure of A Truncated Nipah Virus L Protein Bound By Phosphoprotein Tetramer (pdb code 9iv9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cryo-Em Structure of A Truncated Nipah Virus L Protein Bound By Phosphoprotein Tetramer, PDB code: 9iv9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Cryo-Em Structure of A Truncated Nipah Virus L Protein Bound By Phosphoprotein Tetramer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of A Truncated Nipah Virus L Protein Bound By Phosphoprotein Tetramer within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1501 b:165.4 occ:1.00 OE2 A:GLU1223 2.2 110.1 1.0 SG A:CYS1191 2.3 119.0 1.0 SG A:CYS1428 2.3 148.8 1.0 SG A:CYS1429 2.3 134.8 1.0 CB A:CYS1191 3.2 94.7 1.0 CD A:GLU1223 3.3 97.1 1.0 CB A:CYS1429 3.5 119.5 1.0 CB A:CYS1428 3.7 134.0 1.0 CA A:CYS1191 3.7 88.1 1.0 N A:CYS1429 3.8 120.2 1.0 CG A:GLU1223 3.8 88.3 1.0 C A:CYS1428 3.9 125.6 1.0 CA A:CYS1428 3.9 129.7 1.0 CA A:CYS1429 4.2 121.0 1.0 NZ A:LYS1024 4.3 88.5 1.0 OE1 A:GLU1223 4.4 94.3 1.0 N A:SER1192 4.4 85.1 1.0 O A:CYS1428 4.5 126.9 1.0 C A:CYS1191 4.6 85.1 1.0 N A:CYS1191 4.8 89.7 1.0 CB A:GLU1223 4.9 80.2 1.0

Zinc binding site 2 out of 2 in the Cryo-Em Structure of A Truncated Nipah Virus L Protein Bound By Phosphoprotein Tetramer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo-Em Structure of A Truncated Nipah Virus L Protein Bound By Phosphoprotein Tetramer within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1502 b:127.0 occ:1.00 NE2 A:HIS1423 2.0 96.7 1.0 ND1 A:HIS1421 2.0 94.7 1.0 SG A:CYS1239 2.3 100.5 1.0 SG A:CYS1236 2.3 106.7 1.0 CB A:CYS1236 2.5 101.1 1.0 CG A:HIS1421 2.8 86.5 1.0 CB A:HIS1421 2.8 83.8 1.0 CE1 A:HIS1423 3.0 96.6 1.0 CD2 A:HIS1423 3.0 85.0 1.0 CE1 A:HIS1421 3.2 91.3 1.0 CB A:CYS1239 3.8 108.7 1.0 CD2 A:HIS1421 4.0 83.3 1.0 CA A:CYS1236 4.0 106.6 1.0 ND1 A:HIS1423 4.1 89.5 1.0 CG A:HIS1423 4.2 81.2 1.0 NE2 A:HIS1421 4.2 88.4 1.0 N A:CYS1239 4.2 107.0 1.0 CA A:HIS1421 4.4 77.3 1.0 CA A:CYS1239 4.6 109.7 1.0 C A:CYS1236 4.7 108.6 1.0 N A:CYS1236 4.8 108.3 1.0 CG A:TYR1246 5.0 88.7 1.0 CD2 A:TYR1246 5.0 88.7 1.0 C A:HIS1421 5.0 77.4 1.0

L.Xue, T.Chang, J.Gui, Z.Li, H.Zhao, B.Zou, J.Lu, M.Li, X.Wen, S.Gao, P.Zhan, L.Rong, L.Feng, P.Gong, J.He, X.Chen, X.Xiong. Cryo-Em Structures of Nipah Virus Polymerase Complex Reveal Highly Varied Interactions Between L and P Proteins Among Paramyxoviruses. Protein Cell 2025.
ISSN: ESSN 1674-8018
PubMed: 39964914
DOI: 10.1093/PROCEL/PWAF014