MolNFT v1 · #81169 · protein
Structural basis for the impact of phosphorylation on plant receptor- like kinase BAK1 activation
3UIM · Brassinosteroid insensitive 1-associated receptor kinase 1: “Structural basis for the impact of phosphorylation on plant receptor- like kinase BAK1 activation”. X-ray diffraction, 1 ligand (ANP), 3 pockets (best druggability 0.63).…
- PDB
- 3UIM
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Brassinosteroid insensitive 1-associated receptor kinase 1
- EC
- 2.7.10.1, 2.7.11.1
- UniProt
- Q94F62
- Ligands
- ANP
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Brassinosteroid insensitive 1-associated receptor kinase 1 (EC 2.7.10.1, 2.7.11.1) | protein | 297 | 35% helix, 14% strand | Q94F62 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 320 | 0.63 | 0.79 | 35 | ANP |
| 2 | 89 | 0.37 | 0.76 | 23 | empty |
| 3 | 74 | 0.33 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 6 modified (phosphorylation).
Compared structures
- 3UIM · Structural basis for the impact of phosphorylation on plant receptor-like kinase BAK1… · the same entry in another collection · chain A against A, TM-score 1.00
- Q94F62 · AlphaFold monomer V2.0 prediction for brassinosteroid insensitive 1-associated receptor… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q94F62
- Elsewhere: RCSB PDB 3UIM · PDBe 3UIM · UniProt Q94F62
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