GL1X · GenesisL1 explorer

Research workbench

Crystal structure of FOXC2 dbd bound to DBE2 DNA

Analyse Crystal structure of FOXC2 dbd bound to DBE2 DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6AKO
Type
protein + DNA
Length
129 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA (5'-D(CP*AP*AP*AP*AP*TP*GP*TP*AP*AP*AP*CP*AP*AP*GP*A)- 3'); DNA…
UniProt
Q99958
Ligands
MG
Pockets
4 · best druggability 0.53

Structure

x-ray diffraction · 3 distinct chains · 44% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADNA (5'-D(CP*AP*AP*AP*AP*TP*GP*TP*AP*AP*AP*CP*AP*AP*GP*A)- 3')dna16——
BDNA (5'-D(TP*CP*TP*TP*GP*TP*TP*TP*AP*CP*AP*TP*TP*TP*TP*G)- 3')dna16——
CForkhead box protein C2protein9744% helix, 11% strandQ99958

Ligands and binding sites

  • MG · Magnesium ion · metal · chains C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12370.530.7726empty
21120.340.7313empty
3740.270.7217empty
4510.270.7514empty

Interfaces

3 interfaces between chains.

  • A–B · 715 Ų buried · 56 hydrogen bonds · nucleic-nucleic
  • B–C · 557 Ų buried · 12 hydrogen bonds · protein-nucleic
  • A–C · 452 Ų buried · 11 hydrogen bonds · protein-nucleic

Compared structures

  • 6AKO · Crystal Structure of FOXC2 DBD Bound to DBE2 DNA · the same entry in another collection · chain A against A, TM-score 1.00
  • Q99958 · AlphaFold monomer V2.0 prediction for forkhead box protein C2 (Q99958) · a predicted model of the same protein · chain C against A, TM-score 0.89

Analyse

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