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Cooperation between the intrinsically disordered and ordered regions of SPT6 regulates nucleosome and pol II ctd binding, and nucleosome assembly

Analyse Cooperation between the intrinsically disordered and ordered regions of SPT6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7O6B
Type
protein
Length
879 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcription elongation factor SPT6
UniProt
P23615
Pockets
14 · best druggability 0.68

Structure

electron microscopy · 1 distinct chain · 53% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscription elongation factor SPT6protein87953% helix, 8% strandP23615

Pockets

14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14750.680.7948empty
23850.660.8036empty
32520.570.7833empty
4750.550.8618empty
51830.520.7825empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 7O6B · Cooperation between the intrinsically disordered and ordered regions of Spt6 regulates… · the same entry in another collection · chain A against A, TM-score 1.00
  • P23615 · AlphaFold monomer V2.0 prediction for transcription elongation factor SPT6 (P23615) · a predicted model of the same protein · chain A against A, TM-score 0.97

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