4M7C: TRF2-binding motif of SLX4

Crystal structure of the TRF2-binding motif of SLX4 in complex with the TRFH domain of TRF2. Determined by X-ray diffraction at 2.05 Å resolution. Released 25 Sept 2013.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,665
Mol. weight: 49.84 kDa
Released: 25 Sept 2013

Explore 4M7C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4M7C contains 24 α-helices and 0 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	48-69	22
α-helix	73-86	14
α-helix	95-111	17
α-helix	128-142	15
α-helix	147-167	21
α-helix	171-181	11
α-helix	189-201	13
α-helix	207-210	4
α-helix	214-226	13
α-helix	232-234	3
α-helix	235-243	9

Chain B: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	47-69	23
α-helix	73-86	14
α-helix	95-111	17
α-helix	128-142	15
α-helix	147-167	21
α-helix	171-182	12
α-helix	189-201	13
α-helix	207-210	4
α-helix	214-226	13
α-helix	232-234	3
α-helix	235-243	9

Chains C and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	500-503	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Telomeric repeat-binding factor 2	A, B	protein	200	Homo sapiens	Q15554 (AlphaFold model)
Peptide from Structure-specific endonuclease subunit SLX4	C, D	protein	13	Homo sapiens	Q8IY92 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4M7C_1 Telomeric repeat-binding factor 2 (chains A, B)
EARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLLRVM
QCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAAVII
CIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKMLRF
LESHLDDAEPYLLTMAKKAL

Sequence of entity 2 (C, D), FASTA

>4M7C_2 Peptide from Structure-specific endonuclease subunit SLX4 (chains C, D)
SRGLEVSHRLAPW

Primary citation

SLX4 Assembles a Telomere Maintenance Toolkit by Bridging Multiple Endonucleases with Telomeres. Wan, B., Yin, J., Horvath, K. et al. Cell Rep (2013) 4:861-869. DOI 10.1016/j.celrep.2013.08.017 · PubMed

Other PDB entries of the same protein (UniProt Q15554 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3SJM 1.35 Å, Crystal Structure Analysis of TRF2-Dbd-DNA complex
1W0U 1.8 Å, hTRF2 DNA-binding domain in complex with telomeric DNA.
3K6G 1.95 Å, Crystal structure of Rap1 and TRF2 complex
6J67 2.05 Å, Crystal structure of the compound 34 in a complex with TRF2
3BU8 2.15 Å, Crystal Structure of TRF2 TRFH domain and TIN2 peptide complex
7C5D 2.15 Å, Crystal structure of TRF2 TRFH domain in complex with a MCPH1 peptide
1H6P 2.2 Å, Dimeristion domain from human TRF2
5XYF 2.2 Å, Crystal structure of the human TIN2-TPP1-TRF2 telomeric complex
4RQI 2.44 Å, Structure of TRF2/RAP1 secondary interaction binding site
3BUA 2.5 Å, Crystal Structure of TRF2 TRFH domain and APOLLO peptide complex
9Q9K 2.59 Å, Cryo-EM structure of human Mre11-Rad50 (MR) complex bound to DNA and telomeric factor…
9Q9J 2.71 Å, Cryo-EM structure of human Mre11-Rad50-Nbs1 (MRN) complex bound to DNA and telomeric…

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