Research workbench
Fmrp N-terminal domain
Analyse Fmrp N-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QVZ
- Type
- protein
- Length
- 398 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fragile X mental retardation protein 1
- UniProt
- Q06787
- Pockets
- 5 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fragile X mental retardation protein 1 | protein | 194 | 22% helix, 36% strand | Q06787 |
| B | Fragile X mental retardation protein 1 | protein | 204 | 22% helix, 34% strand | Q06787 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.62 | 0.87 | 25 | empty |
| 2 | 284 | 0.53 | 0.75 | 36 | EDO |
| 3 | 120 | 0.42 | 0.76 | 26 | empty |
| 4 | 51 | 0.40 | 0.81 | 12 | empty |
| 5 | 57 | 0.29 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 667 Ų buried · 5 hydrogen bonds · 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 Q06787
- Elsewhere: RCSB PDB 4QVZ · PDBe 4QVZ · UniProt Q06787
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.