Research workbench
Complex of the yersinia enterocolitica type III secretion proteins yscx and yscy
Analyse Complex of the yersinia enterocolitica type III secretion proteins yscx and yscy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QII
- Type
- protein
- Length
- 186 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein yscy; Yop proteins translocation protein X
- UniProt
- P0C2N2, P0C2N4
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein yscy | protein | 110 | 77% helix, 0% strand | P0C2N2 |
| B | Yop proteins translocation protein X | protein | 76 | 74% helix, 0% strand | P0C2N4 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.34 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1726 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (methylation).
Compared structures
- 7QII · Complex of the Yersinia enterocolitica Type III secretion proteins YscX and YscY · the same entry in another collection · chain A against A, TM-score 1.00
- P0C2N2 · AlphaFold monomer V2.0 prediction for chaperone protein yscy (P0C2N2) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P0C2N4 · AlphaFold monomer V2.0 prediction for yop proteins translocation protein X (P0C2N4) · a predicted model of the same protein · chain B against A, TM-score 0.63
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 P0C2N2
- Every structure of UniProt P0C2N4
- Elsewhere: RCSB PDB 7QII · PDBe 7QII · UniProt P0C2N2 · UniProt P0C2N4
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