Research workbench
Structure of the shaft pilin Spa2 from Corynebacterium glutamicum
Analyse Structure of the shaft pilin Spa2 from Corynebacterium glutamicum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WOI
- Type
- protein
- Length
- 858 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.73
- Source
- Corynebacterium glutamicum ATCC 14067
- Molecule
- Spa2
- UniProt
- A0A223G2M9
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · resolution 2.73 · 1 distinct chain · 5% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Spa2 | protein | 429 | 5% helix, 44% strand | A0A223G2M9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.75 | 0.97 | 22 | empty |
| 2 | 573 | 0.62 | 0.74 | 56 | empty |
| 3 | 294 | 0.54 | 0.75 | 42 | GOL |
| 4 | 300 | 0.53 | 0.74 | 32 | EDO |
| 5 | 63 | 0.33 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 224 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 A0A223G2M9
- Elsewhere: RCSB PDB 7WOI · PDBe 7WOI · UniProt A0A223G2M9
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