MolNFT v1 · #61975 · protein
Structure of an N-terminal truncation of deinococcus radiodurans RECD2
3E1S · Exodeoxyribonuclease V, subunit recd: “Structure of an N-terminal truncation of deinococcus radiodurans RECD2”. X-ray diffraction, 6 pockets (best druggability 0.70). MolNFT v1 #61975 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3E1S
- Type
- protein
- Length
- 517 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exodeoxyribonuclease V, subunit recd
- UniProt
- Q9RT63
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exodeoxyribonuclease V, subunit recd | protein | 517 | 41% helix, 19% strand | Q9RT63 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 751 | 0.70 | 0.77 | 78 | empty |
| 2 | 281 | 0.65 | 0.82 | 31 | empty |
| 3 | 152 | 0.48 | 0.78 | 22 | empty |
| 4 | 81 | 0.37 | 0.76 | 20 | empty |
| 5 | 85 | 0.37 | 0.76 | 13 | empty |
Compared structures
- 3E1S · Structure of an N-terminal truncation of Deinococcus radiodurans RecD2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9RT63 · AlphaFold monomer V2.0 prediction for ATP-dependent recd-like DNA helicase (Q9RT63) · 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 Q9RT63
- Elsewhere: RCSB PDB 3E1S · PDBe 3E1S · UniProt Q9RT63
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.