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Human huntingtin-HAP40 complex structure

Analyse Human huntingtin-HAP40 complex structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6EZ8
Type
protein
Length
2,621 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Huntingtin; Factor VIII intron 22 protein
UniProt
P42858, P23610
Pockets
20 · best druggability 0.90

Structure

electron microscopy · 2 distinct chains · 46% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHuntingtinprotein235347% helix, 0% strandP42858
BFactor VIII intron 22 proteinprotein26842% helix, 0% strandP23610

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18180.900.93132empty
211910.840.85122empty
31320.790.9630empty
41350.780.9646empty
52640.780.9130empty

Interfaces

1 interface between chains.

  • A–B · 5656 Ų buried · 40 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 6EZ8 · Human Huntingtin-HAP40 complex structure · the same entry in another collection · chain B against B, TM-score 1.00
  • P23610 · AlphaFold monomer V2.0 prediction for 40-kda huntingtin-associated protein (P23610) · a predicted model of the same protein · chain B against A, TM-score 0.95

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