Research workbench
Crystal structure of drosophila hexameric C3PO formed by truncated translin and trax
Analyse Crystal structure of drosophila hexameric C3PO formed by truncated translin and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RIU
- Type
- protein
- Length
- 599 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Translin; Translin associated factor X, isoform B
- UniProt
- Q7JVK6, Q8INE1
- Pockets
- 9 · best druggability 0.65
Structure
x-ray diffraction · 3 distinct chains · 76% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translin | protein | 206 | 77% helix, 1% strand | Q7JVK6 |
| B | Translin | protein | 203 | 77% helix, 1% strand | Q7JVK6 |
| C | Translin associated factor X, isoform B | protein | 190 | 75% helix, 0% strand | Q8INE1 |
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.65 | 0.95 | 18 | empty |
| 2 | 439 | 0.62 | 0.76 | 55 | empty |
| 3 | 125 | 0.60 | 0.85 | 26 | empty |
| 4 | 292 | 0.60 | 0.78 | 40 | empty |
| 5 | 75 | 0.58 | 0.88 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1292 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 810 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 124 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 3RIU · Crystal structure of Drosophila hexameric C3PO formed by truncated Translin and Trax · 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 Q7JVK6
- Every structure of UniProt Q8INE1
- Elsewhere: RCSB PDB 3RIU · PDBe 3RIU · UniProt Q7JVK6 · UniProt Q8INE1
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