3BUA: TRF2 TRFH domain and APOLLO peptide complex

Crystal Structure of TRF2 TRFH domain and APOLLO peptide complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 19 Feb 2008.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 8
Atoms: 7,148
Mol. weight: 112.23 kDa
Released: 19 Feb 2008

Explore 3BUA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BUA contains 50 α-helices and 0 β-strands across 7 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: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	45-69	25
α-helix	73-86	14
α-helix	94-96	3
α-helix	98-111	14
α-helix	128-142	15
α-helix	147-167	21
α-helix	171-181	11
α-helix	188-200	13
α-helix	207-210	4
α-helix	214-226	13
α-helix	232-234	3
α-helix	235-243	9

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	45-69	25
α-helix	73-86	14
α-helix	94-96	3
α-helix	98-111	14
α-helix	128-143	16
α-helix	147-167	21
α-helix	171-177	7
α-helix	178-182	5
α-helix	188-190	3
α-helix	191-200	10
α-helix	207-210	4
α-helix	214-227	14
α-helix	235-243	9

Chain C: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	45-69	25
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	186-188	3
α-helix	189-200	12
α-helix	207-210	4
α-helix	214-227	14
α-helix	235-244	10

Chain D: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	46-69	24
α-helix	73-87	15
α-helix	98-111	14
α-helix	128-142	15
α-helix	147-166	20
α-helix	171-177	7
α-helix	178-182	5
α-helix	189-201	13
α-helix	207-210	4
α-helix	214-226	13
α-helix	235-241	7

Chains E, F and H: 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, C, D	protein	204	Homo sapiens	Q15554 (AlphaFold model)
DNA cross-link repair 1B protein	E, F, G, H	protein	36	Homo sapiens	Q9H816 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>3BUA_1 Telomeric repeat-binding factor 2 (chains A, B, C, D)
GAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLL
RVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAA
VIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKM
LRFLESHLDDAEPYLLTMAKKALK

Sequence of entity 2 (E, F, G, H), FASTA

>3BUA_2 DNA cross-link repair 1B protein (chains E, F, G, H)
SEFRGLALKYLLTPVNFFQAGYSSRRFDQQVEKYHK

Primary citation

A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins. Chen, Y., Yang, Y., van Overbeek, M. et al. Science (2008) 319:1092-1096. DOI 10.1126/science.1151804 · 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
4M7C 2.05 Å, Crystal structure of the TRF2-binding motif of SLX4 in complex with the TRFH domain of…
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
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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