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NMR based structural model of the UBCH8-ubiquitin complex

Analyse NMR based structural model of the UBCH8-ubiquitin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2KJH
Type
protein
Length
226 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
UBIQUITIN/ISG15-conjugating enzyme E2 L6; Ubiquitin
EC
6.3.2.19
UniProt
O14933, P62988
Pockets
3 · best druggability 0.50

Structure

solution nmr · 2 distinct chains · 28% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUBIQUITIN/ISG15-conjugating enzyme E2 L6 (EC 6.3.2.19)protein15033% helix, 21% strandO14933
BUbiquitinprotein7618% helix, 34% strandP62988

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12120.500.7630empty
2540.310.7615empty
3600.300.7512empty

Interfaces

1 interface between chains.

  • A–B · 374 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 2KJH · NMR based structural model of the UBCH8-UBIQUITIN complex · the same entry in another collection · chain A against A, TM-score 1.00
  • O14933 · AlphaFold monomer V2.0 prediction for UBIQUITIN/ISG15-conjugating enzyme E2 L6 (O14933) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

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