Research workbench
Crystal structure of C-terminal truncated tip-1 (6-113)
Analyse Crystal structure of C-terminal truncated tip-1 (6-113) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DJ3
- Type
- protein
- Length
- 400 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TAX1-binding protein 3
- UniProt
- Q9DBG9
- Pockets
- 8 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 16% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | TAX1-binding protein 3 | protein | 100 | 16% helix, 38% strand | Q9DBG9 |
| B | TAX1-binding protein 3 | protein | 101 | 14% helix, 36% strand | Q9DBG9 |
| D | TAX1-binding protein 3 | protein | 99 | 19% helix, 34% strand | Q9DBG9 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.70 | 0.92 | 23 | empty |
| 2 | 302 | 0.57 | 0.77 | 41 | empty |
| 3 | 147 | 0.44 | 0.75 | 21 | empty |
| 4 | 82 | 0.37 | 0.76 | 17 | empty |
| 5 | 73 | 0.33 | 0.75 | 17 | empty |
Interfaces
5 interfaces between chains.
- B–C · 409 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 365 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 320 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 213 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 189 Ų buried · 1 hydrogen bond · 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 Q9DBG9
- Elsewhere: RCSB PDB 3DJ3 · PDBe 3DJ3 · UniProt Q9DBG9
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