Structure analysis

Cryo-EM structure of Nipah virus L-P (H1165Y) polymerase complex

Electron Microscopy
3.01Å resolution
Source organism: Henipavirus nipahense
Assembly composition:
hetero hexamer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero hexamer
Accessible surface area: 69875.22 Å2
Buried surface area: 14163.1 Å2
Dissociation area: 1,296.35 Å2
Dissociation energy (ΔGdiss): 3.2 kcal/mol
Dissociation entropy (TΔSdiss): 11.77 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-282583

Macromolecules

Chain: A
Length: 2244 amino acids
Theoretical weight: 257.59 KDa
Source organism: Henipavirus nipahense
Expression system: Spodoptera
UniProt:
  • Canonical: Q997F0 (Residues: 1-2244; Coverage: 100%)
Gene name: L
Pfam:
PDBe-KB: UniProt Coverage View: Q997F0  
122442004006008001,0001,2001,4001,6001,8002,0002,200
 
10002000
UniProt
Q997F0
Chains
Secondary structure
Ligand binding sites
Interaction interfaces
Sequence conservation

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Chains: C, D, E, F, G
Length: 709 amino acids
Theoretical weight: 78.39 KDa
Source organism: Henipavirus nipahense
Expression system: Spodoptera
UniProt:
  • Canonical: Q9IK91 (Residues: 1-709; Coverage: 100%)
Gene name: P/V/C
Pfam:
PDBe-KB: UniProt Coverage View: Q9IK91  
1709100200300400500600700
 
200400600
UniProt
Q9IK91
Chains
Secondary structure
Flexibility predictions
Interaction interfaces
Sequence conservation

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