› 2lam

Solution NMR

Three-dimensional structure of the cyclotide Cter M

Released:
DOI: 10.2210/pdb2lam/pdb
PDB entry 2lam coloured by chain, ensemble of 20 models, front view.
PDB entry 2lam coloured by chain, ensemble of 20 models, side view.
PDB entry 2lam coloured by chain, ensemble of 20 models, top view.
Source organism: Clitoria ternatea
Primary publication:
Discovery of an unusual biosynthetic origin for circular proteins in legumes.
Poth AG, Colgrave ML, Lyons RE, Daly NL, Craik DJ
Proc Natl Acad Sci U S A 108 10127-32 (2011)
PMID: 21593408

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160985 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclotide cter-M Chain: A
Molecule details ›
Chain: A
Length: 29 amino acids
Theoretical weight: 3.08 KDa
Source organism: Clitoria ternatea
Expression system: Not provided
UniProt:
  • Canonical: P86899 (Residues: 25-53; Coverage: 28%)
Sequence domains: Cyclotide family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 51%
Refinement method: torsion angle dynamics
Expression system: Not provided

Quick links

Citations

24 review citations

Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.
Arnison et al. (2013)
23 more

6 mentions without citation

Plant antimicrobial peptides: structures, functions, and applications.
Li et al. (2021)
5 more