Research workbench
Human ARGONAUTE2 helix-7 mutant
Analyse Human ARGONAUTE2 helix-7 mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WEA
- Type
- protein + RNA
- Length
- 772 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein argonaute-2; RNA (5'-R(P*AP*AP*AP*AP*AP*AP*AP*U)-3')
- EC
- 3.1.26.-
- UniProt
- Q9UKV8
- Ligands
- IPH
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein argonaute-2 (EC 3.1.26.-) | protein | 764 | 31% helix, 28% strand | Q9UKV8 |
| B | RNA (5'-R(P*AP*AP*AP*AP*AP*AP*AP*U)-3') | rna | 8 | — | — |
Ligands and binding sites
- IPH · Phenol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 457 | 0.73 | 0.83 | 47 | empty |
| 2 | 376 | 0.64 | 0.79 | 34 | empty |
| 3 | 114 | 0.51 | 0.82 | 23 | empty |
| 4 | 85 | 0.41 | 0.78 | 21 | empty |
| 5 | 112 | 0.40 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1378 Ų buried · 36 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 Q9UKV8
- Elsewhere: RCSB PDB 5WEA · PDBe 5WEA · UniProt Q9UKV8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.