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DNA recognition is mediated by conformational transition and by DNA bending

Analyse DNA recognition is mediated by conformational transition and by DNA bending in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1LJM
Type
protein
Length
228 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RUNX1 transcription factor
UniProt
Q01196
Ligands
CL
Pockets
2 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARUNX1 transcription factorprotein1140% helix, 41% strandQ01196
BRUNX1 transcription factorprotein1140% helix, 39% strandQ01196

Ligands and binding sites

  • CL · Chloride ion · ion · 5 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11940.620.8331empty
21270.390.7426empty

Interfaces

1 interface between chains.

  • A–B · 667 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 1LJM · DNA recognition is mediated by conformational transition and by DNA bending · the same entry in another collection · chain A against A, TM-score 1.00
  • Q01196 · AlphaFold monomer V2.0 prediction for runt-related transcription factor 1 (Q01196) · a predicted model of the same protein · chain B against A, TM-score 0.95

Analyse

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