MolNFT v1 · #102068 · protein + RNA
Complete human RNase L in complex with biological activators.
4OAU · 2-5A-dependent ribonuclease: “Complete human RNase L in complex with biological activators.”. X-ray diffraction, 2 ligands (ADP, MG), 7 pockets (best druggability 0.63). MolNFT v1 #102068 on GenesisL1: 3D structure, binding sites…
- PDB
- 4OAU
- Type
- protein + RNA
- Length
- 695 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-5A-dependent ribonuclease; RNA (5'-R(P*A*AP*A)-2')
- EC
- 3.1.26.-
- UniProt
- Q05823
- Ligands
- ADP, MG
- Pockets
- 7 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | 2-5A-dependent ribonuclease (EC 3.1.26.-) | protein | 692 | 46% helix, 8% strand | Q05823 |
| A | RNA (5'-R(P*A*AP*A)-2') | rna | 3 | — | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.63 | 0.82 | 33 | ADP, MG |
| 2 | 242 | 0.59 | 0.80 | 23 | empty |
| 3 | 275 | 0.51 | 0.74 | 28 | empty |
| 4 | 85 | 0.36 | 0.76 | 21 | empty |
| 5 | 52 | 0.36 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- C–A · 557 Ų buried · 14 hydrogen bonds · protein-nucleic
Compared structures
- 4OAU · Complete human RNase L in complex with biological activators. · the same entry in another collection · chain C against C, TM-score 1.00
- Q05823 · AlphaFold monomer V2.0 prediction for 2-5A-dependent ribonuclease (Q05823) · a predicted model of the same protein · chain C 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 Q05823
- Elsewhere: RCSB PDB 4OAU · PDBe 4OAU · UniProt Q05823
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