Research workbench
N-terminal fragment of drosophila melanogaster sas-6 (F143D), dimerised via the coiled-coil domain.
Analyse N-terminal fragment of drosophila melanogaster sas-6 (F143D), dimerised via the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AL7
- Type
- protein
- Length
- 416 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spindle assembly abnormal protein 6 homolog
- UniProt
- Q9VAC8
- Ligands
- NO3
- Pockets
- 5 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Spindle assembly abnormal protein 6 homolog | protein | 208 | 39% helix, 33% strand | Q9VAC8 |
Ligands and binding sites
- NO3 · Nitrate ion · ion · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 156 | 0.42 | 0.74 | 22 | empty |
| 2 | 72 | 0.39 | 0.79 | 15 | empty |
| 3 | 142 | 0.39 | 0.73 | 25 | empty |
| 4 | 67 | 0.38 | 0.78 | 11 | empty |
| 5 | 53 | 0.34 | 0.78 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1597 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 5AL7 · N-terminal fragment of Drosophila melanogaster Sas-6 (F143D), dimerised via the… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9VAC8 · AlphaFold monomer V2.0 prediction for spindle assembly abnormal protein 6 homolog (Q9VAC8) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 Q9VAC8
- Elsewhere: RCSB PDB 5AL7 · PDBe 5AL7 · UniProt Q9VAC8
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