Research workbench
Structural insight into brassinosteroid perception by BRI1
Analyse Structural insight into brassinosteroid perception by BRI1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RGZ
- Type
- protein
- Length
- 745 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein brassinosteroid insensitive 1
- EC
- 2.7.10.1, 2.7.11.1
- UniProt
- O22476
- Ligands
- BLD, NAG, SO4
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein brassinosteroid insensitive 1 (EC 2.7.10.1, 2.7.11.1) | protein | 745 | 16% helix, 23% strand | O22476 |
Ligands and binding sites
- BLD · Brassinolide · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 16 copies · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 243 | 0.60 | 0.79 | 20 | BLD |
| 2 | 175 | 0.53 | 0.79 | 31 | empty |
| 3 | 51 | 0.44 | 0.85 | 15 | empty |
Modifications
Observed in the structure: 8 disulfide, 8 glycan (disulfide, N-glycosylation).
Compared structures
- 3RGZ · Structural insight into brassinosteroid perception by BRI1 · the same entry in another collection · chain A against A, TM-score 1.00
- O22476 · AlphaFold monomer V2.0 prediction for protein brassinosteroid insensitive 1 (O22476) · a predicted model of the same protein · chain A against A, TM-score 0.99
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
- Elsewhere: RCSB PDB 3RGZ · PDBe 3RGZ · UniProt O22476
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