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Crystal structure of UBE2K and K48-linked di-ubiquitin complex

Analyse Crystal structure of UBE2K and K48-linked di-ubiquitin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IF1
Type
protein
Length
550 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin-conjugating enzyme E2 K; Ubiquitin
EC
2.3.2.23
UniProt
P61086, P0CG47
Pockets
2 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BUbiquitin-conjugating enzyme E2 K (EC 2.3.2.23)protein19945% helix, 13% strandP61086
C, DUbiquitinprotein7620% helix, 29% strandP0CG47

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18520.690.7577empty
21220.490.7930empty

Interfaces

5 interfaces between chains.

  • A–D · 447 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 431 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 210 Ų buried · 2 hydrogen bonds · protein-protein
  • C–D · 72 Ų buried · 1 hydrogen bond · protein-protein
  • A–C · 70 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 isopeptide (isopeptide).

Compared structures

  • 6IF1 · Crystal structure of Ube2K and K48-linked di-ubiquitin complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P61086 · AlphaFold monomer V2.0 prediction for ubiquitin-conjugating enzyme E2 K (P61086) · a predicted model of the same protein · chain A against A, TM-score 0.99

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