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Crystal structure of the DNA-binding domain of human ETV1.

Analyse Crystal structure of the DNA-binding domain of human ETV1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4AVP
Type
protein
Length
372 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ets translocation variant 1
UniProt
P50549
Pockets
1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DEts translocation variant 1protein9349% helix, 15% strandP50549

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 2 copies · chains B, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18190.730.7887empty

Interfaces

5 interfaces between chains.

  • C–D · 854 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 843 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 372 Ų buried · 3 hydrogen bonds · protein-protein
  • B–D · 337 Ų buried · 1 hydrogen bond · protein-protein
  • B–C · 31 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4AVP · Crystal structure of the DNA-binding domain of human ETV1. · the same entry in another collection · chain D against D, TM-score 1.00
  • P50549 · AlphaFold monomer V2.0 prediction for ets translocation variant 1 (P50549) · a predicted model of the same protein · chain B against A, TM-score 0.97

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