Research workbench
Crystal structure of ynaf (universal stress protein F) from salmonella typhimurium
Analyse Crystal structure of ynaf (universal stress protein F) from salmonella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R2L
- Type
- protein
- Length
- 278 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Universal stress protein F
- UniProt
- P67091
- Ligands
- ATP, MG, CL
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Universal stress protein F | protein | 142 | 42% helix, 23% strand | P67091 |
| B | Universal stress protein F | protein | 136 | 46% helix, 22% strand | P67091 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.65 | 0.85 | 25 | MG, ATP, EDO |
| 2 | 225 | 0.64 | 0.83 | 35 | MG, ATP |
Interfaces
1 interface between chains.
- A–B · 876 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 4R2L · Crystal structure of YnaF (Universal Stress Protein F) from Salmonella typhimurium · the same entry in another collection · chain A against A, TM-score 1.00
- P67091 · AlphaFold monomer V2.0 prediction for universal stress protein F (P67091) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P67091
- Elsewhere: RCSB PDB 4R2L · PDBe 4R2L · UniProt P67091
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