Research workbench
3D structure of dotu from francisella novicida
Analyse 3D structure of dotu from francisella novicida in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ACK
- Type
- protein
- Length
- 305 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tssl
- UniProt
- A0Q7H7
- Ligands
- BR
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tssl | protein | 152 | 73% helix, 0% strand | A0Q7H7 |
| B | Tssl | protein | 153 | 75% helix, 0% strand | A0Q7H7 |
Ligands and binding sites
- BR · Bromide ion · ion · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 6 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 461 | 0.65 | 0.77 | 46 | EDO |
| 2 | 101 | 0.39 | 0.76 | 17 | EDO |
Interfaces
1 interface between chains.
- A–B · 270 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4ACK · 3D Structure of DotU from Francisella novicida · the same entry in another collection · chain A against A, 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 A0Q7H7
- Elsewhere: RCSB PDB 4ACK · PDBe 4ACK · UniProt A0Q7H7
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