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Crystal structure of orsay virus delta protein N-terminal fragment (aa 1-101)

Analyse Crystal structure of orsay virus delta protein N-terminal fragment (aa 1-101) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5W82
Type
protein
Length
504 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein delta
UniProt
E9KNV6
Pockets
4 · best druggability 0.88

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
C, B, D, EProtein deltaprotein10143% helix, 31% strandE9KNV6
AProtein deltaprotein10043% helix, 31% strandE9KNV6

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13840.880.9570empty
2720.760.9820empty
3700.750.9720empty
4630.730.9620empty

Interfaces

10 interfaces between chains.

  • C–D · 3402 Ų buried · 53 hydrogen bonds · protein-protein
  • E–A · 3347 Ų buried · 55 hydrogen bonds · protein-protein
  • C–B · 3330 Ų buried · 50 hydrogen bonds · protein-protein
  • B–A · 3329 Ų buried · 53 hydrogen bonds · protein-protein
  • D–E · 3321 Ų buried · 48 hydrogen bonds · protein-protein

Compared structures

  • 5W82 · Crystal structure of Orsay virus delta protein N-terminal fragment (aa 1-101) · the same entry in another collection · chain C against C, TM-score 1.00

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