Research workbench
Crystal structure of the SPA17 docking and dimerization domain from danio rerio
Analyse Crystal structure of the SPA17 docking and dimerization domain from danio rerio in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MY4
- Type
- protein
- Length
- 264 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sperm autoantigenic protein 17
- UniProt
- F1QK17
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Sperm autoantigenic protein 17 | protein | 66 | 52% helix, 0% strand | F1QK17 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.44 | 0.74 | 18 | empty |
| 2 | 162 | 0.42 | 0.73 | 18 | empty |
Interfaces
2 interfaces between chains.
- B–D · 1095 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 1087 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 7MY4 · Crystal Structure of the SPA17 Docking and Dimerization Domain from Danio rerio · the same entry in another collection · chain A against A, TM-score 1.00
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 F1QK17
- Elsewhere: RCSB PDB 7MY4 · PDBe 7MY4 · UniProt F1QK17
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