Research workbench
Structure of the C-terminal domain of tnse double mutant - A453V/D523N
Analyse Structure of the C-terminal domain of tnse double mutant - A453V/D523N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5D16
- Type
- protein
- Length
- 318 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transposon TN7 transposition protein tnse
- UniProt
- P05845
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transposon TN7 transposition protein tnse | protein | 161 | 35% helix, 23% strand | P05845 |
| B | Transposon TN7 transposition protein tnse | protein | 157 | 34% helix, 24% strand | P05845 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 337 | 0.63 | 0.79 | 60 | empty |
| 2 | 80 | 0.45 | 0.80 | 16 | GOL |
| 3 | 90 | 0.43 | 0.79 | 18 | empty |
| 4 | 122 | 0.42 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 501 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5D16 · Structure of the C-terminal domain of TnsE double mutant - A453V/D523N · the same entry in another collection · chain A against A, TM-score 1.00
- P05845 · AlphaFold monomer V2.0 prediction for transposon TN7 transposition protein tnse (P05845) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 5D16 · PDBe 5D16 · UniProt P05845
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