Research workbench
Structural basis for 3' end recognition of nucleic acids by the drosophila argonaute 2 paz domain
Analyse Structural basis for 3' end recognition of nucleic acids by the drosophila… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T2S
- Type
- protein + DNA
- Length
- 125 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-D(*CP*TP*CP*AP*C)-3'; Argonaute 2
- UniProt
- Q9VUQ5
Structure
solution nmr · 2 distinct chains · 23% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | 5'-D(*CP*TP*CP*AP*C)-3' | dna | 2 | — | — |
| A | Argonaute 2 | protein | 123 | 23% helix, 32% strand | Q9VUQ5 |
Interfaces
1 interface between chains.
- B–A · 385 Ų buried · 9 hydrogen bonds · protein-nucleic
Compared structures
- 1T2S · Structural basis for 3' end recognition of nucleic acids by the Drosophila Argonaute 2… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9VUQ5 · AlphaFold monomer V2.0 prediction for protein argonaute-2 (Q9VUQ5) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 Q9VUQ5
- Elsewhere: RCSB PDB 1T2S · PDBe 1T2S · UniProt Q9VUQ5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.