Research workbench
Human suppressor of fused (N-terminal domain)
Analyse Human suppressor of fused (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
- 1M1L
- Type
- protein
- Length
- 940 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Suppressor of fused
- UniProt
- Q9UMX1
- Pockets
- 11 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Suppressor of fused | protein | 236 | 29% helix, 24% strand | Q9UMX1 |
| C, D | Suppressor of fused | protein | 234 | 29% helix, 24% strand | Q9UMX1 |
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 807 | 0.72 | 0.78 | 86 | empty |
| 2 | 197 | 0.66 | 0.84 | 31 | empty |
| 3 | 215 | 0.65 | 0.83 | 33 | empty |
| 4 | 321 | 0.56 | 0.76 | 33 | empty |
| 5 | 222 | 0.56 | 0.79 | 36 | empty |
Interfaces
3 interfaces between chains.
- A–D · 897 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 882 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 717 Ų buried · 17 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 Q9UMX1
- Elsewhere: RCSB PDB 1M1L · PDBe 1M1L · UniProt Q9UMX1
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