Research workbench
Structure of the activated ROQ1 resistosome directly recognizing the pathogen effector xopq (tir domains)
Analyse Structure of the activated ROQ1 resistosome directly recognizing the pathogen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JLX
- Type
- protein
- Length
- 664 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disease resistance protein ROQ1
- EC
- 3.2.2.6
- UniProt
- A0A290U7C4
- Pockets
- 7 · best druggability 0.77
Structure
electron microscopy · 1 distinct chain · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, C, A, D | Disease resistance protein ROQ1 (EC 3.2.2.6) | protein | 166 | 49% helix, 11% strand | A0A290U7C4 |
Pockets
7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1149 | 0.77 | 0.79 | 103 | empty |
| 2 | 655 | 0.75 | 0.81 | 77 | empty |
| 3 | 618 | 0.75 | 0.82 | 69 | empty |
| 4 | 864 | 0.74 | 0.78 | 82 | empty |
| 5 | 345 | 0.66 | 0.81 | 54 | empty |
Interfaces
5 interfaces between chains.
- C–A · 204 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 199 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 166 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 165 Ų buried · 2 hydrogen bonds · protein-protein
- B–A · 11 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7JLX · Structure of the activated Roq1 resistosome directly recognizing the pathogen effector… · 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 A0A290U7C4
- Elsewhere: RCSB PDB 7JLX · PDBe 7JLX · UniProt A0A290U7C4
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