Research workbench
Structure of the rep associates tyrosine transposase bound to a rep hairpin
Analyse Structure of the rep associates tyrosine transposase bound to a rep hairpin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ER8
- Type
- protein + DNA
- Length
- 197 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tnparep for protein; DNA (32-mer)
- UniProt
- Q47152
- Ligands
- NI
- Pockets
- 6 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tnparep for protein | protein | 165 | 36% helix, 17% strand | Q47152 |
| B | DNA (32-mer) | dna | 32 | — | — |
Ligands and binding sites
- NI · Nickel (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.54 | 0.81 | 21 | empty |
| 2 | 79 | 0.42 | 0.79 | 14 | empty |
| 3 | 107 | 0.36 | 0.74 | 23 | empty |
| 4 | 65 | 0.36 | 0.78 | 12 | empty |
| 5 | 51 | 0.30 | 0.77 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 1502 Ų buried · 51 hydrogen bonds · protein-nucleic
Compared structures
- 4ER8 · Structure of the REP associates tyrosine transposase bound to a REP hairpin · the same entry in another collection · chain A against A, TM-score 1.00
- Q47152 · AlphaFold monomer V2.0 prediction for rep-associated tyrosine transposase (Q47152) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q47152
- Elsewhere: RCSB PDB 4ER8 · PDBe 4ER8 · UniProt Q47152
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