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MolNFT v1 · #128616 · protein + DNA

Crystal structure of the RIF1 N-terminal domain (RIF1-ntd) from saccharomyces cerevisiae in complex with DNA

5NW5 · Telomere length regulator protein RIF1: “Crystal structure of the RIF1 N-terminal domain (RIF1-ntd) from saccharomyces cerevisiae in complex with DNA”. X-ray diffraction, 20 pockets (best druggability 0.82). MolNFT v1 #128616 on…

PDB
5NW5
Type
protein + DNA
Length
2,230 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Telomere length regulator protein RIF1; DNA (60-mer); DNA (30-mer)
UniProt
P29539
Pockets
20 · best druggability 0.82

Structure

x-ray diffraction · 4 distinct chains · 68% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATelomere length regulator protein RIF1protein108568% helix, 0% strandP29539
BTelomere length regulator protein RIF1protein108568% helix, 0% strandP29539
CDNA (60-mer)dna30——
DDNA (30-mer)dna30——

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12220.820.9531empty
26710.820.8552empty
31930.800.9432empty
44600.800.8757empty
52750.780.9027empty

Interfaces

6 interfaces between chains.

  • A–B · 1512 Ų buried · 27 hydrogen bonds · protein-protein
  • C–D · 1336 Ų buried · 84 hydrogen bonds · nucleic-nucleic
  • B–C · 245 Ų buried · 8 hydrogen bonds · protein-nucleic
  • A–C · 195 Ų buried · 5 hydrogen bonds · protein-nucleic
  • A–D · 137 Ų buried · 2 hydrogen bonds · protein-nucleic

Compared structures

  • 5NW5 · Crystal structure of the Rif1 N-terminal domain (RIF1-NTD) from Saccharomyces cerevisiae… · the same entry in another collection · chain A against A, TM-score 1.00
  • P29539 · AlphaFold monomer V2.0 prediction for telomere length regulator protein RIF1 (P29539) · a predicted model of the same protein · chain A against A, TM-score 0.85

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