Research workbench
Solution structure of the uas domain from human fas-associated factor 1
Analyse Solution structure of the uas domain from human fas-associated factor 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EC4
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fas-associated factor 1
- UniProt
- Q9UNN5
- Pockets
- 2 · best druggability 0.38
Structure
solution nmr · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fas-associated factor 1 | protein | 171 | 47% helix, 14% strand | Q9UNN5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.38 | 0.76 | 18 | empty |
| 2 | 54 | 0.27 | 0.73 | 18 | empty |
Compared structures
- 2EC4 · Solution structure of the UAS domain from human FAS-associated factor 1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UNN5 · AlphaFold monomer V2.0 prediction for fas-associated factor 1 (Q9UNN5) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q9UNN5
- Elsewhere: RCSB PDB 2EC4 · PDBe 2EC4 · UniProt Q9UNN5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.