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Human early B-cell factor 1 (EBF1) IPT/TIG domain

Analyse Human early B-cell factor 1 (EBF1) IPT/TIG domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3MQI
Type
protein
Length
269 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcription factor COE1
UniProt
Q9UH73
Ligands
EMC, TMO
Pockets
1 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BTranscription factor COE1protein900% helix, 56% strandQ9UH73
CTranscription factor COE1protein890% helix, 56% strandQ9UH73

Ligands and binding sites

  • EMC · Ethyl mercury ion · ligand · 6 copies · chains A, B, C
  • TMO · trimethylamine oxide · ligand · chains B, C

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
12600.590.7945empty

Interfaces

3 interfaces between chains.

  • A–B · 598 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 447 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 289 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 3MQI · Human early B-cell factor 1 (EBF1) IPT/TIG domain · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UH73 · AlphaFold monomer V2.0 prediction for transcription factor COE1 (Q9UH73) · a predicted model of the same protein · chain B against A, TM-score 0.94

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