Research workbench
Crystal structure of DVL1-DIX(Y17D) mutant
Analyse Crystal structure of DVL1-DIX(Y17D) mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PZ8
- Type
- protein
- Length
- 660 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Segment polarity protein dishevelled homolog dvl-1
- UniProt
- P51141
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 7 distinct chains · 10% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Segment polarity protein dishevelled homolog dvl-1 | protein | 82 | 11% helix, 40% strand | P51141 |
| B | Segment polarity protein dishevelled homolog dvl-1 | protein | 85 | 16% helix, 44% strand | P51141 |
| C | Segment polarity protein dishevelled homolog dvl-1 | protein | 81 | 11% helix, 43% strand | P51141 |
| D, E | Segment polarity protein dishevelled homolog dvl-1 | protein | 83 | 8% helix, 45% strand | P51141 |
| F | Segment polarity protein dishevelled homolog dvl-1 | protein | 85 | 12% helix, 46% strand | P51141 |
| G | Segment polarity protein dishevelled homolog dvl-1 | protein | 80 | 6% helix, 44% strand | P51141 |
| H | Segment polarity protein dishevelled homolog dvl-1 | protein | 81 | 4% helix, 41% strand | P51141 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.82 | 0.83 | 87 | empty |
| 2 | 74 | 0.46 | 0.82 | 18 | empty |
| 3 | 59 | 0.42 | 0.81 | 13 | empty |
| 4 | 92 | 0.35 | 0.74 | 23 | empty |
| 5 | 58 | 0.34 | 0.77 | 11 | empty |
Interfaces
13 interfaces between chains.
- A–H · 719 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 688 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 683 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 682 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 646 Ų buried · 8 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 P51141
- Elsewhere: RCSB PDB 3PZ8 · PDBe 3PZ8 · UniProt P51141
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