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Crystal structure of rsv epitope scaffold FFL_005

Analyse Crystal structure of rsv epitope scaffold FFL_005 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4L8I
Type
protein
Length
226 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rsv epitope scaffold FFL_005
Pockets
1 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 91% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARsv epitope scaffold FFL_005protein11491% helix, 0% strand—
BRsv epitope scaffold FFL_005protein11290% helix, 0% strand—

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1770.370.7715empty

Interfaces

1 interface between chains.

  • A–B · 892 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 4L8I · Crystal structure of RSV epitope scaffold FFL_005 · the same entry in another collection · chain A against A, TM-score 1.00

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