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NMR studies of human general transcription factor tfiib: dynamics and interaction with VP16 activation domain, 20 structures

Analyse NMR studies of human general transcription factor tfiib: dynamics and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TFB
Type
protein
Length
206 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tfiib
UniProt
Q00403
Pockets
3 · best druggability 0.38

Structure

solution nmr · 1 distinct chain · 51% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATfiibprotein20651% helix, 0% strandQ00403

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1910.380.7616empty
2560.320.7610empty
3610.320.7616empty

Compared structures

  • 1TFB · NMR studies of human general transcription factor tfiib: dynamics and interaction with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q00403 · AlphaFold monomer V2.0 prediction for transcription initiation factor iib (Q00403) · a predicted model of the same protein · chain A against A, TM-score 0.54

Analyse

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