Research workbench
Crystal structure of folded and partially unfolded forms of aquifex aeolicus ribosomal protein L20
Analyse Crystal structure of folded and partially unfolded forms of aquifex aeolicus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GHJ
- Type
- protein
- Length
- 386 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 50S ribosomal protein L20
- UniProt
- O67086
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | 50S ribosomal protein L20 | protein | 101 | 73% helix, 0% strand | O67086 |
| B, E | 50S ribosomal protein L20 | protein | 92 | 74% helix, 0% strand | O67086 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, E, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 755 | 0.67 | 0.75 | 72 | SO4 |
| 2 | 133 | 0.45 | 0.77 | 23 | SO4 |
| 3 | 109 | 0.42 | 0.77 | 21 | SO4 |
| 4 | 83 | 0.30 | 0.72 | 17 | SO4 |
| 5 | 53 | 0.30 | 0.76 | 10 | empty |
Interfaces
6 interfaces between chains.
- B–E · 1586 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 1460 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 575 Ų buried · 1 hydrogen bond · protein-protein
- A–E · 571 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 402 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2GHJ · Crystal structure of folded and partially unfolded forms of Aquifex aeolicus ribosomal… · the same entry in another collection · chain A against A, TM-score 1.00
- O67086 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L20 (O67086) · a predicted model of the same protein · chain A against A, TM-score 0.71
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 O67086
- Elsewhere: RCSB PDB 2GHJ · PDBe 2GHJ · UniProt O67086
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