1FEX: Myb-domain of human RAP1

Solution structure of myb-domain of human RAP1. Determined by solution NMR. Released 19 Sept 2001.

Method: Solution NMR
Chains: 1
Atoms: 469
Mol. weight: 6.66 kDa
Released: 19 Sept 2001

Explore 1FEX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FEX contains 3 α-helices and 0 β-strands across 1 chain. 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: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	7-19	13
α-helix	31-38	8
α-helix	47-56	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
TRF2-interacting telomeric RAP1 protein	A	protein	59		Q9NYB0 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1FEX_1 TRF2-INTERACTING TELOMERIC RAP1 PROTEIN (chains A)
GRIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSLTQHSWQSLKDRYLKHLRG

Primary citation

NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains. Hanaoka, S., Nagadoi, A., Yoshimura, S. et al. J Mol Biol (2001) 312:167-175. DOI 10.1006/jmbi.2001.4924 · PubMed

Other PDB entries of the same protein (UniProt Q9NYB0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3K6G 1.95 Å, Crystal structure of Rap1 and TRF2 complex
4RQI 2.44 Å, Structure of TRF2/RAP1 secondary interaction binding site
8RD4 3.58 Å, Telomeric RAP1:DNA-PK complex
7OZ0 Solution structure of the N-terminal domain of human telomeric Repeat-binding factor…

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