MolNFT v1 · #188413 · protein + DNA
Structure of human TREX1-DNA complex
7TQQ · Three-prime repair exonuclease 1: “Structure of human TREX1-DNA complex”. X-ray diffraction, 15 pockets (best druggability 0.64). MolNFT v1 #188413 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7TQQ
- Type
- protein + DNA
- Length
- 914 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Three-prime repair exonuclease 1; DNA (5'-D(P*TP*TP*GP*GP*CP*CP*GP*GP*CP*CP*AP*TP*C)-3')
- EC
- 3.1.11.2
- UniProt
- Q9NSU2
- Pockets
- 15 · best druggability 0.64
Structure
x-ray diffraction · 7 distinct chains · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Three-prime repair exonuclease 1 (EC 3.1.11.2) | protein | 212 | 43% helix, 18% strand | Q9NSU2 |
| B | Three-prime repair exonuclease 1 (EC 3.1.11.2) | protein | 213 | 41% helix, 17% strand | Q9NSU2 |
| C, H | DNA (5'-D(P*TP*TP*GP*GP*CP*CP*GP*GP*CP*CP*AP*TP*C)-3') | dna | 16 | — | — |
| D | DNA (5'-D(P*TP*TP*GP*GP*CP*CP*GP*GP*CP*CP*AP*TP*C)-3') | dna | 15 | — | — |
| E | Three-prime repair exonuclease 1 (EC 3.1.11.2) | protein | 214 | 40% helix, 17% strand | Q9NSU2 |
| F | Three-prime repair exonuclease 1 (EC 3.1.11.2) | protein | 215 | 41% helix, 17% strand | Q9NSU2 |
| G | DNA (5'-D(P*TP*TP*GP*GP*CP*CP*GP*GP*CP*CP*AP*TP*C)-3') | dna | 13 | — | — |
Pockets
15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 326 | 0.64 | 0.80 | 33 | empty |
| 2 | 452 | 0.64 | 0.77 | 47 | empty |
| 3 | 401 | 0.63 | 0.78 | 52 | empty |
| 4 | 123 | 0.55 | 0.84 | 17 | empty |
| 5 | 252 | 0.53 | 0.76 | 19 | empty |
Interfaces
7 interfaces between chains.
- E–F · 1660 Ų buried · 43 hydrogen bonds · protein-protein
- A–B · 1649 Ų buried · 45 hydrogen bonds · protein-protein
- F–H · 870 Ų buried · 15 hydrogen bonds · protein-nucleic
- B–D · 816 Ų buried · 14 hydrogen bonds · protein-nucleic
- A–C · 791 Ų buried · 17 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 Q9NSU2
- Elsewhere: RCSB PDB 7TQQ · PDBe 7TQQ · UniProt Q9NSU2
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