Research workbench
Crystal structure of BRI1 SUD1 (GLY643GLU) bound to brassinolide
Analyse Crystal structure of BRI1 SUD1 (GLY643GLU) bound to brassinolide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LSA
- Type
- protein
- Length
- 743 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein brassinosteroid insensitive 1
- UniProt
- O22476
- Ligands
- BLD, NAG, BMA, MAN
- Pockets
- 4 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein brassinosteroid insensitive 1 | protein | 743 | 17% helix, 23% strand | O22476 |
Ligands and binding sites
- BLD · Brassinolide · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 3 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 184 | 0.55 | 0.79 | 20 | BLD |
| 2 | 56 | 0.55 | 0.90 | 24 | empty |
| 3 | 126 | 0.47 | 0.79 | 28 | empty |
| 4 | 53 | 0.33 | 0.78 | 14 | empty |
Modifications
Observed in the structure: 8 disulfide, 7 glycan (disulfide, N-glycosylation).
Compared structures
- 4LSA · Crystal structure of BRI1 sud1 (Gly643Glu) bound to brassinolide · 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 0.98
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 4LSA · PDBe 4LSA · UniProt O22476
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