Research workbench
Solution structure of a chaperone in type III secretion system
Analyse Solution structure of a chaperone in type III secretion system in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M1N
- Type
- protein
- Length
- 214 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type III secretion system filament chaperone cesa
- UniProt
- I2YZH3
- Pockets
- 4 · best druggability 0.61
Structure
solution nmr · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Type III secretion system filament chaperone cesa | protein | 107 | 74% helix, 0% strand | I2YZH3 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.61 | 0.92 | 16 | empty |
| 2 | 334 | 0.56 | 0.75 | 32 | empty |
| 3 | 205 | 0.56 | 0.79 | 25 | empty |
| 4 | 67 | 0.47 | 0.83 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1536 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2M1N · Solution structure of a chaperone in type III secretion system · the same entry in another collection · chain B against B, 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 I2YZH3
- Elsewhere: RCSB PDB 2M1N · PDBe 2M1N · UniProt I2YZH3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.