GL1X · GenesisL1 explorer

Research workbench

Structure of rb tumor suppressor bound to the transactivation domain of E2F-2

Analyse Structure of rb tumor suppressor bound to the transactivation domain of E2F-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1N4M
Type
protein
Length
731 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Retinoblastoma pocket; Transcription factor E2F2
UniProt
Q14209
Pockets
13 · best druggability 0.82

Structure

x-ray diffraction · 4 distinct chains · 65% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARetinoblastoma pocketprotein34568% helix, 1% strand—
BRetinoblastoma pocketprotein33867% helix, 2% strand—
C, DTranscription factor E2F2protein1817% helix, 0% strandQ14209
ETranscription factor E2F2protein120% helix, 0% strandQ14209

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111240.820.8376empty
2900.570.8619empty
31260.400.7518empty
4680.380.7815empty
5910.360.7515empty

Interfaces

4 interfaces between chains.

  • A–C · 1210 Ų buried · 26 hydrogen bonds · protein-protein
  • A–B · 1199 Ų buried · 22 hydrogen bonds · protein-protein
  • B–D · 1151 Ų buried · 24 hydrogen bonds · protein-protein
  • B–E · 548 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 1N4M · Structure of Rb tumor suppressor bound to the transactivation domain of E2F-2 · the same entry in another collection · chain C against C, TM-score 1.00
  • Q14209 · AlphaFold monomer V2.0 prediction for transcription factor E2F2 (Q14209) · a predicted model of the same protein · chain C against A, TM-score 0.29

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.