Research workbench
Crystal structure of the FAF1 UBX domain
Analyse Crystal structure of the FAF1 UBX domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R3M
- Type
- protein
- Length
- 330 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3
- Source
- Homo sapiens
- Molecule
- FAS-associated factor 1
- UniProt
- Q9UNN5
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · resolution 3 · 4 distinct chains · 15% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | FAS-associated factor 1 | protein | 82 | 15% helix, 40% strand | Q9UNN5 |
| A | FAS-associated factor 1 | protein | 84 | 15% helix, 37% strand | Q9UNN5 |
| C | FAS-associated factor 1 | protein | 81 | 15% helix, 38% strand | Q9UNN5 |
| D | FAS-associated factor 1 | protein | 83 | 14% helix, 37% strand | Q9UNN5 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains B, D, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 291 | 0.63 | 0.80 | 41 | empty |
| 2 | 66 | 0.49 | 0.85 | 11 | PO4 |
| 3 | 135 | 0.42 | 0.75 | 29 | empty |
| 4 | 65 | 0.27 | 0.72 | 14 | empty |
Interfaces
6 interfaces between chains.
- B–A · 578 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 512 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 478 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 259 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 245 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
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 3R3M · PDBe 3R3M · UniProt Q9UNN5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.