› 1vak

X-ray diffraction
3.05Å resolution

T=1 capsid structure of Sesbania mosaic virus coat protein deletion mutant CP-N(delta)65

Released:
DOI: 10.2210/pdb1vak/pdb
PDB entry 1vak coloured by chain, front view.
PDB entry 1vak coloured by chain, side view.
PDB entry 1vak coloured by chain, top view.
Source organism: Sesbania mosaic virus
Primary publication:
T=1 capsid structures of Sesbania mosaic virus coat protein mutants: determinants of T=3 and T=1 capsid assembly.
Sangita V, Lokesh GL, Satheshkumar PS, Vijay CS, Saravanan V, Savithri HS, Murthy MR
J Mol Biol 342 987-99 (2004)
PMID: 15342251

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo 60-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190141 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Capsid protein Chain: A
Molecule details ›
Chain: A
Length: 203 amino acids
Theoretical weight: 21.47 KDa
Source organism: Sesbania mosaic virus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9EB06 (Residues: 66-268; Coverage: 76%)
Sequence domains: Viral coat protein (S domain)
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 188.239Å b: 193.954Å c: 269.054Å
α: 90° β: 92.42° γ: 90°
R-values:
R R work R free
0.211 0.211 0.214
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Genome packaging by spherical plant RNA viruses.
Rao AL. (2006)
2 more

1 mention without citation

Tilable nature of virus capsids and the role of topological constraints in natural capsid design.
Mannige et al. (2008)