MolNFT v1 · #163967 · protein
Crystal structure of the UL14-rsfs complex from staphylococcus aureus
6SJ5 · Ribosomal silencing factor rsfs: “Crystal structure of the UL14-rsfs complex from staphylococcus aureus”. X-ray diffraction, 1 ligand (PO4), 3 pockets (best druggability 0.56). MolNFT v1 #163967 on GenesisL1: 3D structure, binding…
- PDB
- 6SJ5
- Type
- protein
- Length
- 470 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosomal silencing factor rsfs; 50S ribosomal protein L14
- UniProt
- A0A0D1JM30, Q2FW16
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 18% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribosomal silencing factor rsfs | protein | 112 | 37% helix, 29% strand | A0A0D1JM30 |
| C | 50S ribosomal protein L14 | protein | 124 | 8% helix, 39% strand | Q2FW16 |
| D | 50S ribosomal protein L14 | protein | 122 | 10% helix, 38% strand | Q2FW16 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.56 | 0.77 | 22 | ACY |
| 2 | 50 | 0.38 | 0.81 | 11 | empty |
| 3 | 56 | 0.27 | 0.73 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–C · 850 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 826 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 501 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6SJ5 · Crystal structure of the uL14-RsfS complex from Staphylococcus aureus · the same entry in another collection · chain A against A, TM-score 1.00
- Q2FW16 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L14 (Q2FW16) · a predicted model of the same protein · chain D 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 A0A0D1JM30
- Every structure of UniProt Q2FW16
- Elsewhere: RCSB PDB 6SJ5 · PDBe 6SJ5 · UniProt A0A0D1JM30 · UniProt Q2FW16
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