MolNFT v1 · #28908 · protein + RNA
Localization and dynamic behavior of ribosomal protein L30E
1YSH · RNA (28-mer): “Localization and dynamic behavior of ribosomal protein L30E”. Electron microscopy, 9 pockets (best druggability 0.72). MolNFT v1 #28908 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1YSH
- Type
- protein + RNA
- Length
- 423 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA (28-mer); RNA (34-mer); RNA (101-mer); Ribosomal protein L30; Ribosomal protein L37A…
- UniProt
- Q5I7K9, Q5QM99
- Pockets
- 9 · best druggability 0.72
Structure
electron microscopy · 6 distinct chains · 47% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA (28-mer) | rna | 28 | — | — |
| F | RNA (34-mer) | rna | 33 | — | — |
| B | RNA (101-mer) | rna | 101 | — | — |
| C | Ribosomal protein L30 | protein | 104 | 37% helix, 13% strand | Q5I7K9 |
| D | Ribosomal protein L37A | protein | 73 | 37% helix, 18% strand | Q5QM99 |
| E | 40S ribosomal protein S13 | protein | 84 | 68% helix, 0% strand | — |
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 585 | 0.72 | 0.80 | 64 | empty |
| 2 | 428 | 0.60 | 0.76 | 37 | empty |
| 3 | 340 | 0.56 | 0.76 | 35 | empty |
| 4 | 424 | 0.54 | 0.74 | 24 | empty |
| 5 | 384 | 0.52 | 0.73 | 35 | empty |
Interfaces
10 interfaces between chains.
- B–E · 974 Ų buried · 34 hydrogen bonds · protein-nucleic
- F–C · 502 Ų buried · 29 hydrogen bonds · protein-nucleic
- A–E · 359 Ų buried · 33 hydrogen bonds · protein-nucleic
- C–E · 353 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 275 Ų buried · 3 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 2 disulfide, 1 isopeptide (disulfide, isopeptide).
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 Q5I7K9
- Every structure of UniProt Q5QM99
- Elsewhere: RCSB PDB 1YSH · PDBe 1YSH · UniProt Q5I7K9 · UniProt Q5QM99
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