Research workbench
S. aureus ssbb with 5-fu
Analyse S. aureus ssbb with 5-fu in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DEP
- Type
- protein
- Length
- 201 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Single-stranded DNA-binding protein
- UniProt
- A0A3F2YLU4
- Ligands
- URF
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Single-stranded DNA-binding protein | protein | 99 | 10% helix, 61% strand | A0A3F2YLU4 |
| B | Single-stranded DNA-binding protein | protein | 102 | 10% helix, 55% strand | A0A3F2YLU4 |
Ligands and binding sites
- URF · 5-fluorouracil · ligand · 2 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 | 200 | 0.48 | 0.75 | 28 | empty |
| 2 | 194 | 0.48 | 0.75 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 358 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7DEP · S. aureus SsbB with 5-FU · the same entry in another collection · chain B against B, TM-score 1.00
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 A0A3F2YLU4
- Elsewhere: RCSB PDB 7DEP · PDBe 7DEP · UniProt A0A3F2YLU4
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