MolNFT v1 · #77281 · protein
Crystal structure of T. celer L30E E6A/R92A variant
3RA5 · 50S ribosomal protein L30E: “Crystal structure of T. celer L30E E6A/R92A variant”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.43). MolNFT v1 #77281 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3RA5
- Type
- protein
- Length
- 194 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 50S ribosomal protein L30E
- UniProt
- P29160
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 50S ribosomal protein L30E | protein | 97 | 43% helix, 20% strand | P29160 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.43 | 0.79 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 712 Ų buried · 7 hydrogen bonds · protein-protein
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 P29160
- Elsewhere: RCSB PDB 3RA5 · PDBe 3RA5 · UniProt P29160
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