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Capsid structure of sesbania mosaic virus coat protein deletion mutant RCP(DELTA 48 to 59)

Analyse Capsid structure of sesbania mosaic virus coat protein deletion mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2VQ0
Type
protein
Length
606 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coat protein
UniProt
Q9EB06
Ligands
CA
Pockets
1 · best druggability 0.39

Structure

x-ray diffraction · 3 distinct chains · 20% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACoat proteinprotein19622% helix, 39% strandQ9EB06
BCoat proteinprotein19721% helix, 40% strandQ9EB06
CCoat proteinprotein21318% helix, 39% strandQ9EB06

Ligands and binding sites

  • CA · Calcium ion · metal · 3 copies · chains A, C, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11080.390.7529empty

Interfaces

3 interfaces between chains.

  • A–B · 994 Ų buried · 18 hydrogen bonds · protein-protein
  • A–C · 988 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 978 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 2VQ0 · Capsid structure of Sesbania mosaic virus coat protein deletion mutant rCP(delta 48 to 59) · the same entry in another collection · chain A against A, TM-score 1.00

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