Research workbench
SSCR_L211H
Analyse SSCR_L211H in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YWL
- Type
- protein
- Length
- 331 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein induced by osmotic stress
- EC
- 1.1.1.195
- UniProt
- A3LWG4
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein induced by osmotic stress (EC 1.1.1.195) | protein | 331 | 43% helix, 15% strand | A3LWG4 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 611 | 0.69 | 0.77 | 61 | empty |
| 2 | 90 | 0.51 | 0.83 | 23 | empty |
| 3 | 80 | 0.37 | 0.76 | 13 | empty |
Compared structures
- 5YWL · SsCR_L211H · 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 A3LWG4
- Elsewhere: RCSB PDB 5YWL · PDBe 5YWL · UniProt A3LWG4
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