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Crystal Structure of mTEAD with a VGL4 Tertiary Structure Mimetic

Analyse Crystal Structure of mTEAD with a VGL4 Tertiary Structure Mimetic in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SBA
Type
protein
Length
232 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.3
Source
Mus musculus; SYNTHETIC CONSTRUCT
Molecule
Transcriptional enhancer factor TEF-3; Vestigial like 4 (Drosophila), isoform CRA_a
UniProt
Q62296, Q3TQI9
Ligands
ACE
Pockets
3 · best druggability 0.32

Structure

x-ray diffraction · resolution 1.3 · 2 distinct chains · 25% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscriptional enhancer factor TEF-3protein21219% helix, 50% strandQ62296
BVestigial like 4 (Drosophila), isoform CRA_aprotein2090% helix, 0% strandQ3TQI9

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A, B
  • GOL · Glycerol · additive · 5 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1660.320.7520empty
2550.280.7315GOL
3580.260.7316empty

Interfaces

1 interface between chains.

  • A–B · 541 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 isopeptide, 1 modified (covalent ligand, isopeptide, nonstandard).

Compared structures

  • 6SBA · Crystal structure of mtead with a VGL4 tertiary structure mimetic · the same entry in another collection · chain A against A, TM-score 1.00
  • Q62296 · AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-3 (Q62296) · a predicted model of the same protein · chain A against A, TM-score 0.95

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