4RQI: TRF2/RAP1 secondary interaction binding site

Structure of TRF2/RAP1 secondary interaction binding site. Determined by X-ray diffraction at 2.44 Å resolution. Released 10 Feb 2016.

Method
X-ray diffraction
Resolution
2.44 Å
Organism
Homo sapiens
Chains
8
Atoms
7,031
Mol. weight
103.19 kDa
Ligands
MG
Released
10 Feb 2016

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

Secondary structure: helices and β-sheets

4RQI contains 48 α-helices and 2 β-strands across 6 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

ElementResiduesLengthSheet
α-helix46-6924
α-helix73-8614
α-helix95-11117
α-helix128-14215
α-helix147-16721
α-helix171-18212
α-helix186-1883
α-helix189-20113
α-helix207-2104
α-helix214-22613
α-helix232-2343
α-helix235-24410
Chain B: 12 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix47-6923
α-helix73-8614
α-helix95-11117
α-helix128-14215
α-helix147-16721
α-helix171-1777
α-helix178-1825
α-helix189-20113
α-helix207-2104
α-helix214-22613
α-helix232-2343
α-helix235-24410
Chain C: 11 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix45-6925
α-helix73-8614
α-helix95-11117
α-helix128-14215
α-helix147-16721
α-helix171-18212
α-helix189-20113
α-helix207-2104
α-helix214-22613
α-helix231-2344
α-helix235-2417
Chain D: 11 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix45-6925
α-helix73-8614
α-helix96-11116
β-strand11911
α-helix128-14215
α-helix147-16721
α-helix171-1799
α-helix189-20113
α-helix207-2104
α-helix214-22613
α-helix232-2343
α-helix235-24410
Chain E: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix93-975
Chain H: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix97-993
β-strand10511

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Telomeric repeat-binding factor 2A, B, C, Dprotein203Homo sapiensQ15554 (AlphaFold model)
Telomeric repeat-binding factor 2-interacting protein 1E, F, G, Hprotein18Homo sapiensQ9NYB0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4RQI_1 Telomeric repeat-binding factor 2 (chains A, B, C, D)
AGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLLR
VMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAAV
IICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKML
RFLESHLDDAEPYLLTMAKKALK
Sequence of entity 2 (E, F, G, H), FASTA
>4RQI_2 Telomeric repeat-binding factor 2-interacting protein 1 (chains E, F, G, H)
ENRERLELEAYRLGPASA

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Water and common crystallization additives (GOL) are not listed.

Primary citation

A higher-order entity formed by the flexible assembly of RAP1 with TRF2. Gaullier, G., Miron, S., Pisano, S. et al. Nucleic Acids Res (2016) 44:1962-1976. DOI 10.1093/nar/gkv1531 · PubMed

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

Browse structure collections

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