Research workbench
Pre-formed plant receptor ERL1-tmm complex
Analyse Pre-formed plant receptor ERL1-tmm complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XJX
- Type
- protein
- Length
- 5,454 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein too many mouths; Lrr receptor-like SERINE/THREONINE-protein kinase ERL1
- EC
- 2.7.11.1
- UniProt
- Q9SSD1, C0LGW6
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, F, D, L, H, J | Protein too many mouths | protein | 365 | 18% helix, 23% strand | Q9SSD1 |
| K, G, A, I, B, E | Lrr receptor-like SERINE/THREONINE-protein kinase ERL1 (EC 2.7.11.1) | protein | 544 | 20% helix, 21% strand | C0LGW6 |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 785 | 0.82 | 0.85 | 103 | empty |
| 2 | 785 | 0.80 | 0.84 | 97 | empty |
| 3 | 786 | 0.80 | 0.84 | 101 | empty |
| 4 | 1024 | 0.78 | 0.80 | 116 | empty |
| 5 | 693 | 0.78 | 0.83 | 83 | empty |
Interfaces
16 interfaces between chains.
- K–L · 1813 Ų buried · 25 hydrogen bonds · protein-protein
- J–I · 1812 Ų buried · 26 hydrogen bonds · protein-protein
- F–E · 1803 Ų buried · 26 hydrogen bonds · protein-protein
- H–G · 1801 Ų buried · 23 hydrogen bonds · protein-protein
- D–B · 1787 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 30 disulfide (disulfide).
Compared structures
- 5XJX · Pre-formed plant receptor ERL1-TMM complex · the same entry in another collection · chain E against E, 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 Q9SSD1
- Every structure of UniProt C0LGW6
- Elsewhere: RCSB PDB 5XJX · PDBe 5XJX · UniProt Q9SSD1 · UniProt C0LGW6
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