› 5l1m

X-ray diffraction
2.75Å resolution

CASKIN2 SAM domain tandem

Released:
DOI: 10.2210/pdb5l1m/pdb
PDB entry 5l1m coloured by chain, front view.
PDB entry 5l1m coloured by chain, side view.
PDB entry 5l1m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein.
Smirnova E, Kwan JJ, Siu R, Gao X, Zoidl G, Demeler B, Saridakis V, Donaldson LW
Cell Commun Signal 14 17 (2016)
PMID: 27549312

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186774 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caskin-2 Chain: A
Molecule details ›
Chain: A
Length: 184 amino acids
Theoretical weight: 20.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WXE0 (Residues: 483-633; Coverage: 13%)
Gene names: CASKIN2, KIAA1139
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
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: P6522
Unit cell:
a: 96.46Å b: 96.46Å c: 119.17Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.247 0.245 0.265
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Plant SAM-Domain Proteins Start to Reveal Their Roles.
Denay et al. (2017)
1 more

1 mention without citation

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