Research workbench
Crystal structure of full-length human suppressor of fused (sufu)
Analyse Crystal structure of full-length human suppressor of fused (sufu) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BL8
- Type
- protein
- Length
- 1,461 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic protein, suppressor of fused homolog
- UniProt
- P0AEX9, Q9UMX1
- Ligands
- GLC
- Pockets
- 15 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding periplasmic protein, suppressor of fused homolog | protein | 727 | 36% helix, 23% strand | P0AEX9, Q9UMX1 |
| B | Maltose-binding periplasmic protein, suppressor of fused homolog | protein | 734 | 37% helix, 24% strand | P0AEX9, Q9UMX1 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 938 | 0.78 | 0.80 | 76 | empty |
| 2 | 446 | 0.75 | 0.84 | 42 | GLC |
| 3 | 412 | 0.72 | 0.83 | 37 | GLC |
| 4 | 374 | 0.68 | 0.81 | 40 | empty |
| 5 | 188 | 0.66 | 0.85 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 699 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4BL8 · Crystal structure of full-length human Suppressor of fused (SUFU) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UMX1 · AlphaFold monomer V2.0 prediction for suppressor of fused homolog (Q9UMX1) · a predicted model of the same protein · chain A against A, TM-score 0.50
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 Q9UMX1
- Elsewhere: RCSB PDB 4BL8 · PDBe 4BL8 · UniProt P0AEX9 · UniProt Q9UMX1
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