GL1X · GenesisL1 explorer

Research workbench

Crystal structure of abin-1 uban in complex with two M1-linked di- ubiquitins

Analyse Crystal structure of abin-1 uban in complex with two M1-linked di- ubiquitins in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6N6R
Type
protein
Length
433 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin; TNFAIP3-interacting protein 1
UniProt
P0CG48, Q9WUU8
Pockets
2 · best druggability 0.56

Structure

x-ray diffraction · 4 distinct chains · 46% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitinprotein14824% helix, 36% strandP0CG48
BTNFAIP3-interacting protein 1protein6896% helix, 0% strandQ9WUU8
DTNFAIP3-interacting protein 1protein6797% helix, 0% strandQ9WUU8
CUbiquitinprotein15021% helix, 36% strandP0CG48

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12670.560.7733empty
21080.340.7216empty

Interfaces

5 interfaces between chains.

  • B–D · 1869 Ų buried · 17 hydrogen bonds · protein-protein
  • A–D · 834 Ų buried · 15 hydrogen bonds · protein-protein
  • B–C · 753 Ų buried · 14 hydrogen bonds · protein-protein
  • D–C · 613 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 562 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 6N6R · Crystal structure of ABIN-1 UBAN in complex with two M1-linked di-ubiquitins · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9WUU8 · AlphaFold monomer V2.0 prediction for TNFAIP3-interacting protein 1 (Q9WUU8) · a predicted model of the same protein · chain D against A, TM-score 0.92

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.