Research workbench
Structure of the C-terminal domain of tnse at 2.85 resolution
Analyse Structure of the C-terminal domain of tnse at 2.85 resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5D17
- Type
- protein
- Length
- 1,894 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transposon TN7 transposition protein tnse
- UniProt
- P05845
- Pockets
- 19 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, M | Transposon TN7 transposition protein tnse | protein | 159 | 32% helix, 26% strand | P05845 |
| B, C, E, F, G, I, L | Transposon TN7 transposition protein tnse | protein | 158 | 34% helix, 26% strand | P05845 |
| D, K | Transposon TN7 transposition protein tnse | protein | 157 | 34% helix, 26% strand | P05845 |
| H | Transposon TN7 transposition protein tnse | protein | 156 | 31% helix, 26% strand | P05845 |
Pockets
19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 936 | 0.73 | 0.77 | 109 | empty |
| 2 | 679 | 0.70 | 0.78 | 70 | empty |
| 3 | 618 | 0.68 | 0.77 | 73 | empty |
| 4 | 267 | 0.57 | 0.77 | 33 | empty |
| 5 | 316 | 0.56 | 0.76 | 45 | empty |
Interfaces
25 interfaces between chains.
- C–D · 682 Ų buried · 13 hydrogen bonds · protein-protein
- I–K · 663 Ų buried · 13 hydrogen bonds · protein-protein
- A–E · 626 Ų buried · 13 hydrogen bonds · protein-protein
- H–M · 620 Ų buried · 13 hydrogen bonds · protein-protein
- B–F · 598 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 5D17 · Structure of the C-terminal domain of TnsE at 2.85 resolution · the same entry in another collection · chain M against M, 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 P05845
- Elsewhere: RCSB PDB 5D17 · PDBe 5D17 · UniProt P05845
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