› 2lmr

Solution NMR

Solution structure of the first sam domain of odin

Released:
DOI: 10.2210/pdb2lmr/pdb
PDB entry 2lmr coloured by chain, ensemble of 20 models, front view.
PDB entry 2lmr coloured by chain, ensemble of 20 models, side view.
PDB entry 2lmr coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the first Sam domain of Odin and binding studies with the EphA2 receptor.
Mercurio FA, Marasco D, Pirone L, Pedone EM, Pellecchia M, Leone M
Biochemistry 51 2136-45 (2012)
PMID: 22332920

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: 101 amino acids
Theoretical weight: 11.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92625 (Residues: 691-770; Coverage: 7%)
Gene names: ANKS1, ANKS1A, KIAA0229, ODIN
Sequence domains: SAM domain (Sterile alpha motif)
Structure domains: Transcription Factor, Ets-1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 81%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The Structural Dynamics, Complexity of Interactions, and Functions in Cancer of Multi-SAM Containing Proteins.
Clements et al. (2023)
13 other articles

8 mentions without citation

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