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.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1411 | — | 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
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q15075
- Elsewhere: UniProt Q15075 · AlphaFold DB Q15075
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