Research workbench
Crystal structure of human smn yg-dimer
Analyse Crystal structure of human smn yg-dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GLI
- Type
- protein
- Length
- 388 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic protein, survival motor neuron protein chimera
- UniProt
- P0AEX9, Q16637
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding periplasmic protein, survival motor neuron protein chimera | protein | 388 | 48% helix, 20% strand | P0AEX9, Q16637 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.56 | 0.76 | 38 | empty |
| 2 | 126 | 0.50 | 0.80 | 26 | empty |
| 3 | 90 | 0.37 | 0.75 | 15 | empty |
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 P0AEX9
- Every structure of UniProt Q16637
- Elsewhere: RCSB PDB 4GLI · PDBe 4GLI · UniProt P0AEX9 · UniProt Q16637
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