5xup

X-ray diffraction
2.1Å resolution

Crystal structure of TRF1 and TERB1

Released:
Source organism: Homo sapiens
Primary publication:
Telomeric TERB1-TRF1 interaction is crucial for male meiosis.
Nat Struct Mol Biol 24 1073-1080 (2017)
PMID: 29083416

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-156975 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Telomeric repeat-binding factor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 202 amino acids
Theoretical weight: 23.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P54274 (Residues: 65-266; Coverage: 46%)
Gene names: PIN2, TERF1, TRBF1, TRF, TRF1
Sequence domains: Telomere repeat binding factor (TRF)
Structure domains: Telomere repeat-binding factor, dimerisation domain
Telomere repeats-binding bouquet formation protein 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 12 amino acids
Theoretical weight: 1.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8NA31 (Residues: 644-655; Coverage: 2%)
Gene names: CCDC79, TERB1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P64
Unit cell:
a: 161.579Å b: 161.579Å c: 45.925Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.177 0.221
Expression system: Escherichia coli BL21(DE3)