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The UBAP1 subunit of escrt-I interacts with ubiquitin via a novel souba domain

Analyse The UBAP1 subunit of escrt-I interacts with ubiquitin via a novel souba domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4AE4
Type
protein
Length
229 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin-associated protein 1
UniProt
Q9NZ09
Ligands
K, NA
Pockets
1 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitin-associated protein 1protein11475% helix, 0% strandQ9NZ09
BUbiquitin-associated protein 1protein11574% helix, 0% strandQ9NZ09

Ligands and binding sites

  • K · Potassium ion · metal · 4 copies · chains A, B
  • NA · Sodium ion · metal · chains B
  • NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 2 copies · chains A, B
  • GOL · Glycerol · additive · chains A

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
17180.680.7676K, NA

Interfaces

1 interface between chains.

  • A–B · 678 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified, 1 disulfide (engineered, nonstandard, disulfide).

Compared structures

  • 4AE4 · The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a novel SOUBA domain · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NZ09 · AlphaFold monomer V2.0 prediction for ubiquitin-associated protein 1 (Q9NZ09) · a predicted model of the same protein · chain A against A, TM-score 0.95

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