Research workbench
Structural insight into bl-induced activation of the BRI1-BAK1 complex
Analyse Structural insight into bl-induced activation of the BRI1-BAK1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M7E
- Type
- protein
- Length
- 1,817 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein brassinosteroid insensitive 1; Brassinosteroid insensitive 1-associated receptor…
- EC
- 2.7.10.1, 2.7.11.1
- UniProt
- O22476, Q94F62
- Ligands
- BLD, NAG, SO4
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 16% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein brassinosteroid insensitive 1 (EC 2.7.10.1, 2.7.11.1) | protein | 733 | 16% helix, 21% strand | O22476 |
| B | Protein brassinosteroid insensitive 1 (EC 2.7.10.1, 2.7.11.1) | protein | 734 | 16% helix, 19% strand | O22476 |
| D, C | Brassinosteroid insensitive 1-associated receptor kinase 1 (EC 2.7.10.1, 2.7.11.1) | protein | 175 | 22% helix, 15% strand | Q94F62 |
Ligands and binding sites
- BLD · Brassinolide · ligand · 2 copies · chains A, C, B, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 961 | 0.79 | 0.81 | 84 | BLD |
| 2 | 1154 | 0.79 | 0.80 | 97 | BLD |
| 3 | 116 | 0.41 | 0.76 | 29 | empty |
| 4 | 114 | 0.37 | 0.74 | 23 | empty |
| 5 | 75 | 0.33 | 0.76 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–C · 838 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 796 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 645 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 6 glycan (disulfide, N-glycosylation).
Compared structures
- 4M7E · Structural insight into BL-induced activation of the BRI1-BAK1 complex · the same entry in another collection · chain C against C, TM-score 1.00
- Q94F62 · AlphaFold monomer V2.0 prediction for brassinosteroid insensitive 1-associated receptor… · a predicted model of the same protein · chain C against A, TM-score 0.98
- O22476 · AlphaFold monomer V2.0 prediction for protein brassinosteroid insensitive 1 (O22476) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 O22476
- Every structure of UniProt Q94F62
- Elsewhere: RCSB PDB 4M7E · PDBe 4M7E · UniProt O22476 · UniProt Q94F62
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