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MolNFT v1 · #91697 · protein

Structural and biophysical characterization of the syk activation switch

4FL2 · Tyrosine-protein kinase syk: “Structural and biophysical characterization of the syk activation switch”. X-ray diffraction, 2 ligands (ANP, MG), 9 pockets (best druggability 0.69). MolNFT v1 #91697 on GenesisL1: 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).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine-protein kinase syk (EC 2.7.10.2)protein55537% helix, 21% strandP43405

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13490.690.8243MG, ANP
22010.630.8326empty
31780.490.7724empty
41630.470.7627empty
5570.440.8314empty

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

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