Research workbench
CRYSTAL STRUCTURE OF a DUF1285 family protein (SPO_0140) FROM SILICIBACTER POMEROYI DSS-3 AT 2.50 A RESOLUTION
Analyse CRYSTAL STRUCTURE OF a DUF1285 family protein (SPO_0140) FROM SILICIBACTER… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RE3
- Type
- protein
- Length
- 367 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.5
- Source
- Silicibacter pomeroyi DSS-3
- Molecule
- Uncharacterized protein
- UniProt
- Q5LWU5
- Pockets
- 6 · best druggability 0.57
Structure
x-ray diffraction · resolution 2.5 · 2 distinct chains · 19% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 183 | 19% helix, 42% strand | Q5LWU5 |
| B | Uncharacterized protein | protein | 184 | 19% helix, 44% strand | Q5LWU5 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.57 | 0.77 | 37 | empty |
| 2 | 100 | 0.53 | 0.83 | 22 | empty |
| 3 | 169 | 0.52 | 0.78 | 38 | GOL |
| 4 | 73 | 0.45 | 0.82 | 16 | empty |
| 5 | 112 | 0.37 | 0.73 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 850 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2RE3 · Crystal structure of a DUF1285 family protein (SPO_0140) from silicibacter pomeroyi dss-3… · 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 Q5LWU5
- Elsewhere: RCSB PDB 2RE3 · PDBe 2RE3 · UniProt Q5LWU5
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