MolNFT v1 · #111585 · protein
Structure of the C. elegans sas-5 coiled coil domain
4YV4 · Spindle assembly abnormal protein 5: “Structure of the C. elegans sas-5 coiled coil domain”. X-ray diffraction, 2 ligands (SO4, PO4), 9 pockets (best druggability 0.72). MolNFT v1 #111585 on GenesisL1: 3D structure, binding sites…
- PDB
- 4YV4
- Type
- protein
- Length
- 427 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spindle assembly abnormal protein 5
- UniProt
- Q20010
- Ligands
- SO4, PO4
- Pockets
- 9 · best druggability 0.72
Structure
x-ray diffraction · 6 distinct chains · 95% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spindle assembly abnormal protein 5 | protein | 47 | 91% helix, 0% strand | Q20010 |
| B | Spindle assembly abnormal protein 5 | protein | 51 | 96% helix, 0% strand | Q20010 |
| C, H | Spindle assembly abnormal protein 5 | protein | 57 | 95% helix, 0% strand | Q20010 |
| D, G | Spindle assembly abnormal protein 5 | protein | 56 | 96% helix, 0% strand | Q20010 |
| E | Spindle assembly abnormal protein 5 | protein | 53 | 94% helix, 0% strand | Q20010 |
| F | Spindle assembly abnormal protein 5 | protein | 50 | 96% helix, 0% strand | Q20010 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains C, D, G, H, E, F
- PO4 · Phosphate ion · ion · 2 copies · chains C, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.72 | 0.89 | 23 | SO4 |
| 2 | 171 | 0.72 | 0.89 | 23 | empty |
| 3 | 257 | 0.71 | 0.85 | 38 | empty |
| 4 | 291 | 0.56 | 0.77 | 32 | empty |
| 5 | 200 | 0.56 | 0.79 | 23 | empty |
Interfaces
18 interfaces between chains.
- B–D · 924 Ų buried · 9 hydrogen bonds · protein-protein
- E–G · 911 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 867 Ų buried · 7 hydrogen bonds · protein-protein
- E–F · 829 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 807 Ų buried · 9 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 Q20010
- Elsewhere: RCSB PDB 4YV4 · PDBe 4YV4 · UniProt Q20010
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