› 2myq

Solution NMR

NMR structure of an Odin-Sam1 fragment

Released:
DOI: 10.2210/pdb2myq/pdb
PDB entry 2myq coloured by chain, ensemble of 20 models, front view.
PDB entry 2myq coloured by chain, ensemble of 20 models, side view.
PDB entry 2myq coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-Sam.
Mercurio FA, Di Natale C, Pirone L, Scognamiglio PL, Marasco D, Pedone EM, Saviano M, Leone M
Chembiochem 16 1629-36 (2015)
PMID: 26120079

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-187710 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ankyrin repeat and SAM domain-containing protein 1A Chain: A
Molecule details ›
Chain: A
Length: 45 amino acids
Theoretical weight: 4.97 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q92625 (Residues: 715-757; Coverage: 4%)
Gene names: ANKS1, ANKS1A, KIAA0229, ODIN
Sequence domains: SAM domain (Sterile alpha motif)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 50%
Refinement method: simulated annealing, torsion angle dynamics
Expression system: Not provided

Quick links

Citations

1 review citation

Self-Assembling Peptides: From Design to Biomedical Applications.
La Manna et al. (2021)
2 other articles

1 mention without citation

Hunting for Novel Routes in Anticancer Drug Discovery: Peptides against Sam-Sam Interactions.
Mercurio et al. (2022)