GL1X · GenesisL1 explorer

MolNFT v1 · #110411 · protein

AlphaFold monomer V2.0 prediction for early endosome antigen 1 (Q15075)

Q15075: “AlphaFold monomer V2.0 prediction for early endosome antigen 1 (Q15075)”. MolNFT v1 #110411 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession
Q15075
Type
protein
Length
1,411 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
UniProt
Q15075

Structure

1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein1411—Q15075

Compared structures

  • 1JOC · EEA1 homodimer of C-terminal fyve domain bound to inositol 1,3-diphosphate · an experimental structure of the same protein · chain A against B, TM-score 0.08
  • 1JOC · EEA1 homodimer of C-terminal FYVE domain bound to inositol 1,3-diphosphate · an experimental structure of the same protein · chain A against B, TM-score 0.08
  • 1HYI · Solution structure of the EEA1 fyve domain complexed with inositol 1,3-bisphosphate · an experimental structure of the same protein · chain A against A, TM-score 0.04
  • 1HYI · Solution structure of the EEA1 fyve domain complexed with inositol 1, 3-bisphosphate · an experimental structure of the same protein · chain A against A, TM-score 0.04
  • 1HYJ · Solution structure of the EEA1 fyve domain · an experimental structure of the same protein · chain A against A, TM-score 0.04
  • 1HYJ · Solution structure of the EEA1 fyve domain · an experimental structure of the same protein · chain A against A, TM-score 0.04
  • 3MJH · Crystal structure of human RAB5A in complex with the C2H2 zinc finger of EEA1 · an experimental structure of the same protein · chain A against B, TM-score 0.02
  • 3MJH · Crystal Structure of Human Rab5A in complex with the C2H2 Zinc Finger of EEA1 · an experimental structure of the same protein · chain A against B, TM-score 0.02

Analyse

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