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Crystal structure of apo-SpuD
Analyse Crystal structure of apo-SpuD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TTK
- Type
- protein
- Length
- 1,020 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.97
- Source
- Pseudomonas aeruginosa
- Molecule
- Polyamine transport protein
- UniProt
- Q9I6J1
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · resolution 2.97 · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Polyamine transport protein | protein | 340 | 47% helix, 17% strand | Q9I6J1 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 998 | 0.74 | 0.77 | 75 | empty |
| 2 | 986 | 0.73 | 0.77 | 81 | empty |
| 3 | 558 | 0.68 | 0.78 | 39 | empty |
| 4 | 407 | 0.61 | 0.76 | 45 | empty |
| 5 | 109 | 0.36 | 0.74 | 16 | empty |
Interfaces
2 interfaces between chains.
- A–C · 464 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 404 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 Q9I6J1
- Elsewhere: RCSB PDB 3TTK · PDBe 3TTK · UniProt Q9I6J1
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