MolNFT v1 · #28274 · protein
The human TREX2 3' exonuclease structure suggests a mechanism for efficient non-processive DNA catalysis
1Y97 · Three prime repair exonuclease 2: “The human TREX2 3' exonuclease structure suggests a mechanism for efficient non-processive DNA catalysis”. X-ray diffraction, 5 pockets (best druggability 0.51). MolNFT v1 #28274 on GenesisL1: 3D…
- PDB
- 1Y97
- Type
- protein
- Length
- 425 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Three prime repair exonuclease 2
- EC
- 3.1.11.2
- UniProt
- Q9BQ50
- Pockets
- 5 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Three prime repair exonuclease 2 (EC 3.1.11.2) | protein | 214 | 43% helix, 18% strand | Q9BQ50 |
| B | Three prime repair exonuclease 2 (EC 3.1.11.2) | protein | 211 | 44% helix, 19% strand | Q9BQ50 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 220 | 0.51 | 0.76 | 24 | empty |
| 2 | 245 | 0.50 | 0.75 | 34 | empty |
| 3 | 140 | 0.41 | 0.74 | 19 | empty |
| 4 | 61 | 0.33 | 0.77 | 15 | empty |
| 5 | 60 | 0.32 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1638 Ų buried · 44 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 1Y97 · The human TREX2 3' exonuclease structure suggests a mechanism for efficient… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BQ50 · AlphaFold monomer V2.0 prediction for three prime repair exonuclease 2 (Q9BQ50) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9BQ50
- Elsewhere: RCSB PDB 1Y97 · PDBe 1Y97 · UniProt Q9BQ50
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