5wqd

X-ray diffraction
3Å resolution

Crystal structure of TRF2 TRFH in complex with an NBS1 peptide

Released:
Source organism: Homo sapiens
Primary publication:
NBS1 Phosphorylation Status Dictates Repair Choice of Dysfunctional Telomeres.
Mol Cell 65 801-817.e4 (2017)
PMID: 28216226

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-130214 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Telomeric repeat-binding factor 2 Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 204 amino acids
Theoretical weight: 23.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15554 (Residues: 84-287; Coverage: 38%)
Gene names: TERF2, TRBF2, TRF2
Sequence domains: Telomere repeat binding factor (TRF)
Structure domains: Telomere repeat-binding factor, dimerisation domain
Nibrin Chains: H, I, J, K, L, M, N
Molecule details ›
Chains: H, I, J, K, L, M, N
Length: 16 amino acids
Theoretical weight: 1.88 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: O60934 (Residues: 423-438; Coverage: 2%)
Gene names: NBN, NBS, NBS1, P95

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21212
Unit cell:
a: 144.616Å b: 153.267Å c: 108.029Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.233 0.284
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided