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I38T mutant of 2009 H1N1 pa endonuclease

Analyse I38T mutant of 2009 H1N1 pa endonuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5VP8
Type
protein
Length
179 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polymerase acidic protein
UniProt
C3W5S0
Ligands
9HD, MN, SO4
Pockets
1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolymerase acidic proteinprotein17953% helix, 13% strandC3W5S0

Ligands and binding sites

  • 9HD · 1-[(3R,5S,7R)-1,5,7,9-tetrakis(2-oxopyrrolidin-1-yl) nonan-3-yl]-1,3-dihydro-2H-pyrrol-2-one · ligand · chains A
  • MN · Manganese (II) ion · metal · chains A
  • SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14350.660.7843empty

Compared structures

  • 5VP8 · I38T mutant of 2009 H1N1 PA Endonuclease · the same entry in another collection · chain A against A, TM-score 1.00

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