› 2lht

Solution NMR

Solution structure of Venturia inaequalis cellophane-induced 1 protein (ViCin1) domains 1 and 2

Released:
DOI: 10.2210/pdb2lht/pdb
PDB entry 2lht coloured by chain, ensemble of 20 models, front view.
PDB entry 2lht coloured by chain, ensemble of 20 models, side view.
PDB entry 2lht coloured by chain, ensemble of 20 models, top view.
Source organism: Venturia inaequalis
Primary publication:
Structure, dynamics and domain organization of the repeat protein Cin1 from the apple scab fungus.
Mesarich CH, Schmitz M, Tremouilhac P, McGillivray DJ, Templeton MD, Dingley AJ
Biochim Biophys Acta 1824 1118-28 (2012)
PMID: 22771296

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellophane-induced protein 1 Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 13.65 KDa
Source organism: Venturia inaequalis
Expression system: Komagataella pastoris
UniProt:
  • Canonical: A8W3P3 (Residues: 26-147; Coverage: 24%)
Gene name: CIN1
Sequence domains: Cellophane-induced 1 (cin1) repeat
Structure domains: DNA polymerase; domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: simulated annealing
Expression system: Komagataella pastoris

Quick links

Citations

1 review citation

NMR spectroscopy on domain dynamics in biomacromolecules.
Shapiro YE. (2013)
2 other articles

1 mention without citation

Repeat-containing protein effectors of plant-associated organisms.
Mesarich et al. (2015)