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Triple mutant sftavn

Analyse Triple mutant sftavn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4J4S
Type
protein
Length
962 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nucleocapsid protein
UniProt
I6WJ72
Ligands
NA
Pockets
8 · best druggability 0.80

Structure

x-ray diffraction · 4 distinct chains · 64% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANucleocapsid proteinprotein24668% helix, 1% strandI6WJ72
BNucleocapsid proteinprotein23862% helix, 2% strandI6WJ72
CNucleocapsid proteinprotein23358% helix, 2% strandI6WJ72
DNucleocapsid proteinprotein24567% helix, 2% strandI6WJ72

Ligands and binding sites

  • NA · Sodium ion · metal · 8 copies · chains A, B, C, D

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

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111420.800.81106empty
29120.790.82104NA
33890.720.8335empty
44400.680.8052empty
51490.460.7732empty

Interfaces

6 interfaces between chains.

  • A–B · 2236 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 1922 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 295 Ų buried · 3 hydrogen bonds · protein-protein
  • B–D · 212 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 145 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 4J4S · Triple mutant SFTAVN · the same entry in another collection · chain A against A, TM-score 1.00

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