Research workbench
Tetr in complex with the tetr-binding RNA-aptamer K1
Analyse Tetr in complex with the tetr-binding RNA-aptamer K1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SY4
- Type
- protein + RNA
- Length
- 400 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetracycline repressor protein class B from transposon TN10; Tetr-binding aptamer K1…
- UniProt
- P04483
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetracycline repressor protein class B from transposon TN10 | protein | 188 | 71% helix, 0% strand | P04483 |
| B | Tetracycline repressor protein class B from transposon TN10 | protein | 176 | 72% helix, 0% strand | P04483 |
| C | Tetr-binding aptamer K1 (43-mer) | rna | 36 | — | — |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 756 | 0.80 | 0.83 | 55 | empty |
| 2 | 684 | 0.77 | 0.82 | 49 | empty |
| 3 | 570 | 0.69 | 0.79 | 50 | empty |
| 4 | 53 | 0.24 | 0.73 | 11 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1701 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 448 Ų buried · 9 hydrogen bonds · protein-nucleic
- A–C · 439 Ų buried · 10 hydrogen bonds · protein-nucleic
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 P04483
- Elsewhere: RCSB PDB 6SY4 · PDBe 6SY4 · UniProt P04483
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