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Crystal structure of the type III secretion chaperone syct from yersinia enterocolitica (crystal form 1)
Analyse Crystal structure of the type III secretion chaperone syct from yersinia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BSI
- Type
- protein
- Length
- 228 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Yopt chaperone syct
- UniProt
- O85243
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Yopt chaperone syct | protein | 114 | 29% helix, 32% strand | O85243 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.45 | 0.79 | 20 | empty |
| 2 | 68 | 0.32 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1103 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 2BSI · Crystal structure of the type III secretion chaperone SycT from Yersinia enterocolitica… · 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 O85243
- Elsewhere: RCSB PDB 2BSI · PDBe 2BSI · UniProt O85243
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