GL1X · GenesisL1 explorer

Research workbench

Structure of FOXG1 DNA binding domain bound to DBE2 DNA site

Analyse Structure of FOXG1 DNA binding domain bound to DBE2 DNA site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7CBY
Type
protein + DNA
Length
132 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA (5'-D(*TP*CP*TP*TP*GP*TP*TP*TP*AP*CP*AP*TP*TP*TP*TP*G)- 3'); DNA…
UniProt
P55316
Pockets
3 · best druggability 0.41

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADNA (5'-D(*TP*CP*TP*TP*GP*TP*TP*TP*AP*CP*AP*TP*TP*TP*TP*G)- 3')dna16——
BDNA (5'-D(*CP*AP*AP*AP*AP*TP*GP*TP*AP*AP*AP*CP*AP*AP*GP*A)- 3')dna16——
CForkhead box protein G1protein10045% helix, 15% strandP55316

Ligands and binding sites

  • PEG · Di(hydroxyethyl)ether · additive · chains A, 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1940.410.7815empty
2970.330.7413empty
3510.220.7113empty

Interfaces

3 interfaces between chains.

  • A–B · 710 Ų buried · 57 hydrogen bonds · nucleic-nucleic
  • A–C · 545 Ų buried · 11 hydrogen bonds · protein-nucleic
  • B–C · 447 Ų buried · 6 hydrogen bonds · protein-nucleic

Compared structures

  • 7CBY · Structure of FOXG1 DNA binding domain bound to DBE2 DNA site · the same entry in another collection · chain A against A, TM-score 1.00
  • P55316 · AlphaFold monomer V2.0 prediction for forkhead box protein G1 (P55316) · a predicted model of the same protein · chain C against A, TM-score 0.98

Analyse

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