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Crystal structure of the fyn SH3 domain in space group C21 at pH 7.5

Analyse Crystal structure of the fyn SH3 domain in space group C21 at pH 7.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7A2J
Type
protein
Length
116 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine-protein kinase fyn
EC
2.7.10.2
UniProt
P06241
Ligands
NA
Pockets
1 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine-protein kinase fyn (EC 2.7.10.2)protein585% helix, 45% strandP06241
BTyrosine-protein kinase fyn (EC 2.7.10.2)protein585% helix, 41% strandP06241

Ligands and binding sites

  • NA · Sodium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1530.280.7417empty

Interfaces

1 interface between chains.

  • A–B · 353 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 7A2J · Crystal structure of the Fyn SH3 domain in space group C21 at pH 7.5 · the same entry in another collection · chain A against A, TM-score 1.00
  • P06241 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase fyn (P06241) · a predicted model of the same protein · chain A against A, TM-score 0.95

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