Research workbench
The first domain of the ribosomal protein L1 from thermus thermophilus
Analyse The first domain of the ribosomal protein L1 from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OV7
- Type
- protein
- Length
- 395 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 50S ribosomal protein L1
- UniProt
- P27150
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 23% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 50S ribosomal protein L1 | protein | 134 | 25% helix, 28% strand | P27150 |
| B | 50S ribosomal protein L1 | protein | 133 | 25% helix, 25% strand | P27150 |
| C | 50S ribosomal protein L1 | protein | 128 | 20% helix, 28% strand | P27150 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 835 | 0.80 | 0.83 | 85 | empty |
| 2 | 114 | 0.61 | 0.86 | 22 | empty |
| 3 | 76 | 0.35 | 0.76 | 18 | empty |
| 4 | 63 | 0.32 | 0.76 | 14 | empty |
Interfaces
3 interfaces between chains.
- B–C · 528 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 432 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 150 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2OV7 · The first domain of the ribosomal protein L1 from Thermus thermophilus · the same entry in another collection · chain A against A, TM-score 1.00
- P27150 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L1 (P27150) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P27150
- Elsewhere: RCSB PDB 2OV7 · PDBe 2OV7 · UniProt P27150
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