MolNFT v1 · #121154 · protein
AlphaFold monomer V2.0 prediction for ets translocation variant 1 (P50549)
P50549: “AlphaFold monomer V2.0 prediction for ets translocation variant 1 (P50549)”. MolNFT v1 #121154 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P50549
- Type
- protein
- Length
- 477 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- UniProt
- P50549
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 477 | — | P50549 |
Compared structures
- 5ILS · Autoinhibited ETV1 · an experimental structure of the same protein · chain A against A, TM-score 0.21
- 5ILS · Autoinhibited ETV1 · an experimental structure of the same protein · chain A against A, TM-score 0.21
- 4BNC · Crystal structure of the DNA-binding domain of human ETV1 complexed with DNA · an experimental structure of the same protein · chain A against A, TM-score 0.20
- 4BNC · Crystal structure of the DNA-binding domain of human ETV1 complexed with DNA · an experimental structure of the same protein · chain A against A, TM-score 0.20
- 4AVP · Crystal structure of the DNA-binding domain of human ETV1. · an experimental structure of the same protein · chain A against B, TM-score 0.19
- 4AVP · Crystal structure of the DNA-binding domain of human ETV1. · an experimental structure of the same protein · chain A against B, TM-score 0.19
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 P50549
- Elsewhere: UniProt P50549 · AlphaFold DB P50549
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.