Research workbench
Fmrp N-terminal domain (R138Q)
Analyse Fmrp N-terminal domain (R138Q) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QW2
- 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
- Ligands
- PB
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fragile X mental retardation protein 1 | protein | 198 | 23% helix, 37% strand | Q06787 |
| B | Fragile X mental retardation protein 1 | protein | 200 | 22% helix, 37% strand | Q06787 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 289 | 0.65 | 0.82 | 36 | empty |
| 2 | 140 | 0.61 | 0.85 | 22 | empty |
| 3 | 63 | 0.35 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 837 Ų buried · 7 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 4QW2 · PDBe 4QW2 · UniProt Q06787
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