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Structural basis for recruitment of UBC12 by an E2-binding domain in NEDD8'S E1

Analyse Structural basis for recruitment of UBC12 by an E2-binding domain in NEDD8'S E1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Y8X
Type
protein
Length
252 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin-conjugating enzyme E2 M; Ubiquitin-activating enzyme E1C
EC
6.3.2.19
UniProt
P61081, Q8TBC4

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitin-conjugating enzyme E2 M (EC 6.3.2.19)protein16030% helix, 20% strandP61081
BUbiquitin-activating enzyme E1Cprotein9227% helix, 29% strandQ8TBC4

Interfaces

1 interface between chains.

  • A–B · 925 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 1Y8X · Structural basis for recruitment of Ubc12 by an E2-binding domain in NEDD8's E1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P61081 · AlphaFold monomer V2.0 prediction for NEDD8-conjugating enzyme UBC12 (P61081) · a predicted model of the same protein · chain A against A, TM-score 0.99
  • Q8TBC4 · AlphaFold monomer V2.0 prediction for NEDD8-activating enzyme E1 catalytic subunit… · a predicted model of the same protein · chain B against A, TM-score 0.96

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