Zinc in PDB 9iva: Cryo-Em Structure of the Full-Length Nipah Virus L Protein Bound By Phosphoprotein Tetramer

All present enzymatic activity of Cryo-Em Structure of the Full-Length 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 the Full-Length Nipah Virus L Protein Bound By Phosphoprotein Tetramer (pdb code 9iva). 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 the Full-Length Nipah Virus L Protein Bound By Phosphoprotein Tetramer, PDB code: 9iva:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Cryo-Em Structure of the Full-Length 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 the Full-Length Nipah Virus L Protein Bound By Phosphoprotein Tetramer within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2301 b:134.1 occ:1.00 SG A:CYS1191 2.3 110.1 1.0 SG A:CYS1428 2.3 135.3 1.0 SG A:CYS1429 2.3 128.6 1.0 OE2 A:GLU1223 2.5 96.5 1.0 N A:CYS1429 3.1 119.8 1.0 CB A:CYS1429 3.4 115.8 1.0 C A:CYS1428 3.4 127.6 1.0 CB A:CYS1428 3.5 134.7 1.0 CB A:CYS1191 3.5 90.5 1.0 CA A:CYS1428 3.5 133.8 1.0 CD A:GLU1223 3.6 94.1 1.0 CA A:CYS1429 3.7 119.2 1.0 CG A:GLU1223 4.0 95.7 1.0 CA A:CYS1191 4.2 83.9 1.0 O A:CYS1428 4.3 128.7 1.0 OE1 A:GLU1223 4.6 91.9 1.0 N A:SER1192 4.8 76.3 1.0 CB A:GLU1223 5.0 93.4 1.0

Zinc binding site 2 out of 2 in the Cryo-Em Structure of the Full-Length 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 the Full-Length Nipah Virus L Protein Bound By Phosphoprotein Tetramer within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2302 b:114.9 occ:1.00 NE2 A:HIS1423 2.0 92.5 1.0 ND1 A:HIS1421 2.0 90.3 1.0 SG A:CYS1239 2.3 101.2 1.0 SG A:CYS1236 2.3 101.5 1.0 CB A:CYS1236 2.6 102.2 1.0 CG A:HIS1421 2.8 84.8 1.0 CB A:HIS1421 3.0 77.5 1.0 CE1 A:HIS1423 3.0 95.0 1.0 CD2 A:HIS1423 3.1 84.9 1.0 CE1 A:HIS1421 3.2 86.0 1.0 CB A:CYS1239 3.7 104.8 1.0 CD2 A:HIS1421 4.0 85.0 1.0 N A:CYS1239 4.1 103.3 1.0 ND1 A:HIS1423 4.1 89.6 1.0 CA A:CYS1236 4.2 105.5 1.0 NE2 A:HIS1421 4.2 87.3 1.0 CG A:HIS1423 4.2 83.3 1.0 CA A:CYS1239 4.4 104.3 1.0 CA A:HIS1421 4.5 70.2 1.0 CG A:TYR1246 4.8 88.4 1.0 C A:CYS1236 4.8 110.9 1.0 CB A:ILE1238 4.9 93.0 1.0 CD2 A:TYR1246 4.9 84.8 1.0 N A:CYS1236 5.0 106.6 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