Research workbench
Structural and biophysical characterization of the syk activation switch
Analyse Structural and biophysical characterization of the syk activation switch in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FL2
- Type
- protein
- Length
- 555 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase syk
- EC
- 2.7.10.2
- UniProt
- P43405
- Ligands
- ANP, MG
- Pockets
- 9 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase syk (EC 2.7.10.2) | protein | 555 | 37% helix, 21% strand | P43405 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.69 | 0.82 | 43 | MG, ANP |
| 2 | 201 | 0.63 | 0.83 | 26 | empty |
| 3 | 178 | 0.49 | 0.77 | 24 | empty |
| 4 | 163 | 0.47 | 0.76 | 27 | empty |
| 5 | 57 | 0.44 | 0.83 | 14 | empty |
Compared structures
- 4FL2 · Structural and Biophysical Characterization of the Syk Activation Switch · the same entry in another collection · chain A against A, TM-score 1.00
- P43405 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase syk (P43405) · 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 P43405
- Elsewhere: RCSB PDB 4FL2 · PDBe 4FL2 · UniProt P43405
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