Research workbench
Crystal structure of FLG22 in complex with the FLS2 and BAK1 ectodomains
Analyse Crystal structure of FLG22 in complex with the FLS2 and BAK1 ectodomains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MN8
- Type
- protein
- Length
- 955 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lrr receptor-like SERINE/THREONINE-protein kinase FLS2; Brassinosteroid insensitive…
- EC
- 2.7.11.1, 2.7.10.1
- UniProt
- Q9FL28, Q94F62
- Ligands
- NAG, SO4
- Pockets
- 7 · best druggability 0.62
Structure
x-ray diffraction · 3 distinct chains · 20% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lrr receptor-like SERINE/THREONINE-protein kinase FLS2 (EC 2.7.11.1) | protein | 759 | 20% helix, 19% strand | Q9FL28 |
| B | Brassinosteroid insensitive 1-associated receptor kinase 1 (EC 2.7.10.1, 2.7.11.1) | protein | 175 | 19% helix, 15% strand | Q94F62 |
| C | FLG22 | protein | 21 | 14% helix, 5% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A, C, B
- SO4 · Sulfate ion · ion · 16 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 387 | 0.62 | 0.77 | 42 | SO4 |
| 2 | 111 | 0.60 | 0.87 | 26 | SO4 |
| 3 | 110 | 0.58 | 0.85 | 19 | empty |
| 4 | 134 | 0.50 | 0.80 | 28 | empty |
| 5 | 100 | 0.42 | 0.78 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1154 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 933 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 183 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 glycan, 3 disulfide (N-glycosylation, disulfide).
Compared structures
- 4MN8 · Crystal structure of flg22 in complex with the FLS2 and BAK1 ectodomains · 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 B against A, TM-score 0.99
- Q9FL28 · AlphaFold monomer V2.0 prediction for lrr receptor-like SERINE/THREONINE-protein kinase… · 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 Q9FL28
- Every structure of UniProt Q94F62
- Elsewhere: RCSB PDB 4MN8 · PDBe 4MN8 · UniProt Q9FL28 · UniProt Q94F62
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