MolNFT v1 · #108838 · protein
Stationary phase survival protein yuic from B.SUBTILIS complexed with nag
4WJT · Uncharacterized protein yuic: “Stationary phase survival protein yuic from B.SUBTILIS complexed with nag”. X-ray diffraction, 2 ligands (3P9, NAG), 2 pockets (best druggability 0.40). MolNFT v1 #108838 on GenesisL1: 3D structure…
- PDB
- 4WJT
- Type
- protein
- Length
- 292 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein yuic
- UniProt
- O32108
- Ligands
- 3P9, NAG
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Uncharacterized protein yuic | protein | 146 | 23% helix, 29% strand | O32108 |
Ligands and binding sites
- 3P9 · (2S)-2-{[(2S)-2-{[(2R)-2-hydroxypropyl]oxy}propyl]oxy}propan-1-ol · ligand · chains B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
- DMS · Dimethyl sulfoxide · additive · 4 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.40 | 0.79 | 26 | NAG |
| 2 | 73 | 0.38 | 0.78 | 21 | NAG |
Interfaces
1 interface between chains.
- A–B · 4139 Ų buried · 62 hydrogen bonds · protein-protein
Compared structures
- 4WJT · Stationary Phase Survival Protein YuiC from B.subtilis complexed with NAG · the same entry in another collection · chain A against A, TM-score 1.00
- O32108 · AlphaFold monomer V2.0 prediction for uncharacterized protein yuic (O32108) · a predicted model of the same protein · chain A against A, TM-score 0.72
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 O32108
- Elsewhere: RCSB PDB 4WJT · PDBe 4WJT · UniProt O32108
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