› 2rst

Solution NMR

NMR structure of the C-terminal domain of EW29

Released:
DOI: 10.2210/pdb2rst/pdb
PDB entry 2rst coloured by chain, ensemble of 20 models, front view.
PDB entry 2rst coloured by chain, ensemble of 20 models, side view.
PDB entry 2rst coloured by chain, ensemble of 20 models, top view.
Source organism: Lumbricus terrestris
Primary publication:
NMR structure and dynamics of the C-terminal domain of R-type lectin from the earthworm Lumbricus terrestris.
Hemmi H, Kuno A, Hirabayashi J
FEBS J 280 70-82 (2013)
PMID: 23122331

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132139 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ricin B lectin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 132 amino acids
Theoretical weight: 14.88 KDa
Source organism: Lumbricus terrestris
Expression system: Escherichia coli
UniProt:
  • Canonical: O96048 (Residues: 130-260; Coverage: 50%)
Sequence domains: Ricin-type beta-trefoil lectin domain
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 94%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Insights into the molecular flexibility of θ-defensins by NMR relaxation analysis.
Conibear et al. (2014)
3 more

2 mentions without citation

NMR structure and dynamics of the C-terminal domain of R-type lectin from the earthworm Lumbricus terrestris.
Hemmi et al. (2013)
1 more