Crystal structure of the RAP1 C-terminal domain (RAP1-rct) in complex with the RAP1 binding module of RIF1 (RIF1-rbm)

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 3% strand (DSSP).

Ligands and binding sites

• EDO · 1,2-ethanediol · additive · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

9 interfaces between chains.

• A–D · 659 Ų buried · 6 hydrogen bonds · protein-protein
• C–F · 656 Ų buried · 5 hydrogen bonds · protein-protein
• B–E · 655 Ų buried · 6 hydrogen bonds · protein-protein
• A–B · 306 Ų buried · 5 hydrogen bonds · protein-protein
• B–C · 264 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

• 4BJT · Crystal structure of the Rap1 C-terminal domain (Rap1-RCT) in complex with the Rap1… · the same entry in another collection · chain F against F, TM-score 1.00
• P11938 · AlphaFold monomer V2.0 prediction for DNA-binding protein RAP1 (P11938) · a predicted model of the same protein · chain A against A, TM-score 0.97
• P29539 · AlphaFold monomer V2.0 prediction for telomere length regulator protein RIF1 (P29539) · a predicted model of the same protein · chain D against A, TM-score 0.58

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P11938
• Every structure of UniProt P29539
• Elsewhere: RCSB PDB 4BJT · PDBe 4BJT · UniProt P11938 · UniProt P29539