1lky

X-ray diffraction
2.3Å resolution

Structure of the wild-type TEL-SAM polymer

Released:
Source organism: Homo sapiens
Primary publication:
Native interface of the SAM domain polymer of TEL.
BMC Struct Biol 2 5 (2002)
PMID: 12193272

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-154338 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcription factor ETV6 Chains: A, C, E
Molecule details ›
Chains: A, C, E
Length: 77 amino acids
Theoretical weight: 9.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P41212 (Residues: 47-123; Coverage: 17%)
Gene names: ETV6, TEL, TEL1
Sequence domains: Sterile alpha motif (SAM)/Pointed domain
Structure domains: Transcription Factor, Ets-1
Transcription factor ETV6 Chains: B, D, F
Molecule details ›
Chains: B, D, F
Length: 77 amino acids
Theoretical weight: 9.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P41212 (Residues: 47-123; Coverage: 17%)
Gene names: ETV6, TEL, TEL1
Sequence domains: Sterile alpha motif (SAM)/Pointed domain
Structure domains: Transcription Factor, Ets-1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 52.752Å b: 60.291Å c: 62.318Å
α: 116.21° β: 98.89° γ: 98.65°
R-values:
R R work R free
0.232 0.232 0.283
Expression system: Escherichia coli