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Crystal structure of interleukin enhancer-binding factor 1 bound to DNA

Analyse Crystal structure of interleukin enhancer-binding factor 1 bound to DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2C6Y
Type
protein + DNA
Length
225 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Forkhead box protein K2; Interleukin 2 promotor
UniProt
Q01167
Ligands
MG
Pockets
3 · best druggability 0.60

Structure

x-ray diffraction · 4 distinct chains · 46% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AForkhead box protein K2protein9846% helix, 10% strandQ01167
BForkhead box protein K2protein9546% helix, 11% strandQ01167
CInterleukin 2 promotordna16——
DInterleukin 2 promotordna16——

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14090.600.7641empty
2940.450.8023empty
3780.350.7715empty

Interfaces

5 interfaces between chains.

  • C–D · 670 Ų buried · 51 hydrogen bonds · nucleic-nucleic
  • A–D · 646 Ų buried · 9 hydrogen bonds · protein-nucleic
  • A–C · 541 Ų buried · 10 hydrogen bonds · protein-nucleic
  • B–D · 446 Ų buried · 8 hydrogen bonds · protein-nucleic
  • B–C · 254 Ų buried · 1 hydrogen bond · protein-nucleic

Compared structures

  • 2C6Y · Crystal structure of interleukin enhancer-binding factor 1 bound to DNA · the same entry in another collection · chain A against A, TM-score 1.00
  • Q01167 · AlphaFold monomer V2.0 prediction for forkhead box protein K2 (Q01167) · a predicted model of the same protein · chain A against A, TM-score 0.96

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