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9 ångström resolution cryo-EM reconstruction structure of semliki forest virus (sfv) and fitting of the capsid protein structure in the EM density

Analyse 9 ångström resolution cryo-EM reconstruction structure of semliki forest virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DYL
Type
protein
Length
596 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nucleocapsid protein
UniProt
P03315

Structure

electron microscopy · 1 distinct chain · 7% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DNucleocapsid proteinprotein1497% helix, 46% strandP03315

Interfaces

2 interfaces between chains.

  • B–D · 696 Ų buried · 62 hydrogen bonds · protein-protein
  • B–C · 505 Ų buried · 37 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 isopeptide (disulfide, isopeptide).

Compared structures

  • 1DYL · 9 ångström resolution cryo-EM reconstruction structure of semliki forest virus (sfv) and… · the same entry in another collection · chain A against A, TM-score 1.00

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