Research workbench
Structure of the heterotrimeric complex which regulates type III secretion needle formation
Analyse Structure of the heterotrimeric complex which regulates type III secretion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UWJ
- Type
- protein
- Length
- 215 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- PSEUDOMONAS AERUGINOSA
- Molecule
- Type III export protein psce; Type III export protein pscf; Type III export protein pscg
- UniProt
- Q9I317, P95434, P95435
- Ligands
- NI
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · resolution 2 · 3 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Type III export protein psce | protein | 70 | 77% helix, 0% strand | Q9I317 |
| F | Type III export protein pscf | protein | 32 | 56% helix, 0% strand | P95434 |
| G | Type III export protein pscg | protein | 113 | 78% helix, 0% strand | P95435 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 3 copies · chains E, G, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 67 | 0.28 | 0.72 | 15 | empty |
Interfaces
3 interfaces between chains.
- F–G · 1301 Ų buried · 13 hydrogen bonds · protein-protein
- E–G · 987 Ų buried · 10 hydrogen bonds · protein-protein
- E–F · 264 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2UWJ · Structure of the heterotrimeric complex which regulates type III secretion needle… · the same entry in another collection · chain E against E, TM-score 1.00
- P95435 · AlphaFold monomer V2.0 prediction for type III export protein pscg (P95435) · a predicted model of the same protein · chain G against A, TM-score 0.97
- Q9I317 · AlphaFold monomer V2.0 prediction for type III export protein psce (Q9I317) · a predicted model of the same protein · chain E against A, TM-score 0.95
- P95434 · AlphaFold monomer V2.0 prediction for type III needle protein pscf (P95434) · a predicted model of the same protein · chain F against A, TM-score 0.51
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 Q9I317
- Every structure of UniProt P95434
- Every structure of UniProt P95435
- Elsewhere: RCSB PDB 2UWJ · PDBe 2UWJ · UniProt Q9I317 · UniProt P95434 · UniProt P95435
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